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8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate

-
-
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
Chromatium sp.
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
catalytic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
mechanism, Fe protein cycle
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme complex dissociation and association kinetics
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
C2H2 inhibition mechanism, structure model
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
MgATP/MgADP-dependent electron and proton transfer kinetics
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
structure of V-containing enzyme form
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
440134, 440140, 440142, 440143, 440144, 440145, 440146, 440147, 440149, 440152, 440157, 440166, 440174
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
440134, 440142, 440143, 440144, 440145, 440146, 440147, 440153, 440159, 440164, 440174, 440180, 440186
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
440134, 440138, 440142, 440143, 440144, 440145, 440146, 440147, 440150, 440153, 440154, 440155, 440156, 440158, 440163, 440166, 440174, 440175, 440178, 440179, 440180, 440181, 440182, 440183, 440184, 440186, 440187, 440189
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
Chromatium sp.
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
Gloeocapsa sp.
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
Cyanobacterium sp.
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Fe protein and MoFe protein are assumed to associate and dissociate to transfer a single electron to the substrates
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic electron flow from Fe protein to substrate via MoFe protein and MoFe protein-cofactor
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
iron-only enzyme is composed of 2 components: FeFe protein and Fe protein
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
Chromatium sp.
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
schematic mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
active site is located on the MoFe cofactor involving residues alphaR96, alphaG69, alphaV70, and alphaH195
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
active site location
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
overall catalytic mechanism, overview, structures of active site metal clusters, interactions of substrate and active site, active site relevant residues are Arg96, Val70, Gly69, and His195, substrate binding mechanism of complex components, mechanism of MgATP hydrolysis and electron transfer, overview
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
the active site is located on the MoFe protein, active site structure and substrate binding mechanism
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
theoretical mechanisms of substrate binding to molybdenum or iron in the FeMo cofactor, modeling
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
first introduction of H at the NFe7MoS9(homocitrate) active site is via a water chain terminating at water 679 to S3B of the my3-S atoms of the active site. Discussion of subsequent movement of the H atoms around the NFe7MoS9(homocitrate) preparatory to the binding and hydrogenation of N2 and other substrates. S2B has a modulatory function and is not an H-entry site
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
reaction mechanism, overview
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
SEPR1 intermediate formed during turnover of the nitrogenase alpha-195Gln MoFe protein with C2H2 in H2O buffers, is a product complex with C2H4 bound as a ferracycle to a single Fe of the FeMo-cofactor active site. CO bridges two Fe of lo-Co, while the C2H4 of SEPR1 binds to one of these. Correlation with Lowe-Thorneley En kinetic state
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
theoretical investigation of the binding of N2 to the Fe7MoS9N(homocitrate)(cysteine)(histidine) active site, calculation of reaction profiles and activation energies for the association and dissociation of N2. An endo-ny1-N2 coordination at Fe6 is most probable
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
reaction mechanism, determination of reaction intermediates, two-step relaxation of the nitrogenase H+/H+ intermediate during step-annealing,both steps show large solvent kinetic isotope effects, step A is the catalytically central state that is activated for N2 binding by the accumulation of 4 electrons, and step B accumulates 2 electrons, overview
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
NO2- reduction by nitrogenase begins with the generation of NO2H bound to a state in which the active-site FeMo-cofactor (M) has accumulated two [e-/H+] (E2), stored as a (bridging) hydride and proton. Proton transfer to NO2H and H2O loss leaves M-[NO+], transfer of the E2 hydride to the [NO+] directly to form HNO bound to FeMo-cofactor is one of two alternative means for avoiding formation of a terminal M-[NO] thermodynamic sink. Mechanism for N2 reduction, detailed overview. NO2- reduction by nitrogenase begins with the generation of NO2H bound to E2, E2 has accumulated two [e-/H+], stored in the form of a hydride bridging between two Fe atoms and a proton bound to sulfur. Transfer of the E2 proton to the -OH of NO2H followed by loss of H2O formally leaves M-[NO+]. Nitrogenase is able to transfer the E2 hydride to [NO+], directly forming HNO bound to FeMo-cofactor at its resting-state redox level and totally avoiding formation of an M-[NO] sink
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
active site is located on the MoFe cofactor involving residues alphaR96, alphaG69, alphaV70, and alphaH195
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
the active site is located on the MoFe protein, active site structure and substrate binding mechanism
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
iron-only enzyme is composed of 2 components: FeFe protein and Fe protein
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
-
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein
-
-
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(VO4)3- + ?
(VO2)+ + ?
-
reduction of vanadium(V) by reduced Fe-protein of enzyme to vanadium(IV), which then probably binds to the nucleotide binding site in place of the Mg2+ which is normally present. The oxidized Fe-protein is unable to reduce vanadate
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
3,3-difluorocyclopropene + dithionite
propene + 2-fluoropropene + ?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
acetylene + ?
ethylene + ?
acetylene + dithionite + H+ + ATP + H2O
ethylene + ?
-
-
-
?
C2H2 + ?
H2 + ?
-
-
-
-
?
CN- + europium(II) diethylenetriaminepentaacetate + H+
?
CO + dithionite + H+
CH4 + C2H6 + C2H4 + C3H6 + C3H8 + ?
CO + europium(II) diethylenetriaminepentaacetate + H+
?
CS2 + ?
H2S + ?
slow turnover
-
-
?
dithionite + H+ + acetylene + ATP
?
dithionite + H+ + N2 + ATP
?
dithionite + H+ + N2 + ATP + CO2
CO + CH4 + C2H6 + C3H6 + C3H8 + C4H8 + C4H10 + ?
-
-
-
-
?
flavodoxin hydroquinone + H+ + N2 + ATP + H2O
?
-
-
-
-
?
hydrazine + reduced ferredoxin
2 NH3 + oxidized ferredoxin
-
-
-
?
hydroxylamine + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
-
-
?
N2 + 10 H+ + 8 e- + 16 ATP
2 NH4+ + H2 + 16 ADP + 16 phosphate
N2 + 4 reduced ferredoxin
hydrazine + 4 oxidized ferredoxin
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
nitrite + 4 reduced ferredoxin + 5 H+
hydroxylamine + H2O + 4 oxidized ferredoxin
-
-
-
?
nitrite + 7 H+ + 12 ATP
NH3 + 2 H2O + 12 ADP + 12 phosphate
overall reaction
-
-
?
nitrite + H+ + ATP + reduced ferredoxin
NH3 + 2 H2O + 12 ADP + 12 phosphate + oxidized ferredoxin
overall reaction
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
reduced ferredoxin + H+ + SCN- + ATP
oxidized ferredoxin + H2S + HCN + ADP + phosphate
-
-
-
?
additional information
?
-
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O

2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
ferredoxin is the main but not the essential electron donor for nitrogenase
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
ferredoxin is the main but not the essential electron donor for nitrogenase
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
active site for acetylene reduction interacts not directly with N2 reduction
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
anaerobic atmosphere
reduction cycle continues until complete reduction of the substrate to ethane
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
Chromatium sp.
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
Cyanobacterium sp.
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
Gloeocapsa sp.
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
3,3-difluorocyclopropene + dithionite

propene + 2-fluoropropene + ?
-
-
major products providing evidence for reductive C-F bond cleavage. Synthesis of propene requires 6 e-/6 H+ and of 2-fluoropropene requires 4 e-/4 H+. In both products, C=C bond cleavage rather than C-C bond cleavage is involved. No selectivity is observed in formation of cis and trans isomers of 1,3-d2-2-fluoropropene, whereas cis-1,3-d2-propene is the predominant 1,3-d2-propene product, indicating that one of the bound reduction intermediates on the pathway to propene is constrained geometrically. Reduction requires both N2ase proteins MoFe and Fe protein, ATP, and an exogenous reductant such as dithionite. A reduction mechanism, consistent with hydride transfer as a key step, is discussed
-
?
3,3-difluorocyclopropene + dithionite
propene + 2-fluoropropene + ?
-
-
major products providing evidence for reductive C-F bond cleavage. Synthesis of propene requires 6 e-/6 H+ and of 2-fluoropropene requires 4 e-/4 H+. In both products, C=C bond cleavage rather than C-C bond cleavage is involved. No selectivity is observed in formation of cis and trans isomers of 1,3-d2-2-fluoropropene, whereas cis-1,3-d2-propene is the predominant 1,3-d2-propene product, indicating that one of the bound reduction intermediates on the pathway to propene is constrained geometrically. Reduction requires both N2ase proteins MoFe and Fe protein, ATP, and an exogenous reductant such as dithionite. A reduction mechanism, consistent with hydride transfer as a key step, is discussed
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP

6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
intermediate is a flavodoxin hydroquinone
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
6 reduced flavodoxin + N2 + 6 H2O + 6 ATP
6 oxidized flavodoxin + 2 NH3 + 6 H+ + 6 ADP + 6 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O

8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
slow enzyme
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
1-propyne, 1-butyne and allene are reduced to the corresponding alkenes
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
Fe protein and MoFe protein are assumed to associate and dissociate to transfer a single electron to the substrates, termed Fe protein cycle, driven by MgATP hydrolysis, with the dissociation of the Fe protein-MoFe protein complex being the rate limiting step of the cycle
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
overall reaction
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Chromatium sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Chromatium sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Chromatium sp.
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Chromatium sp.
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
MgATP-dependent
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cyanobacterium sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cyanobacterium sp.
-
ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cyanobacterium sp.
-
regulation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cyanobacterium sp.
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Gloeocapsa sp.
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
acetylene + ?

ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
acetylene + ?
ethylene + ?
-
-
-
-
?
C2H2 + ?

?
-
-
-
-
?
CN- + europium(II) diethylenetriaminepentaacetate + H+

?
-
-
cofactor-deficient enzyme catalyzes formation of methane, ethane, ethene, propane, propene, butene, butane, pentene, pentane
-
?
CN- + europium(II) diethylenetriaminepentaacetate + H+
?
-
-
cofactor-deficient enzyme catalyzes formation of methane, ethane, ethene, propane, propene, butene, butane, pentene, pentane
-
?
CO + dithionite + H+

CH4 + C2H6 + C2H4 + C3H6 + C3H8 + ?
-
no substrate for wild-type
MoFe subunit mutants V70A and V70G will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane. The rates and ratios of hydrocarbon production from CO can be adjusted by changing the flux of electrons through nitrogenase, by substitution of other amino acids located near the FeMo-cofactor, or by changing the partial pressure of CO. Increasing the partial pressure of CO shifts the product ratio in favor of the longer chain alkanes and alkenes
-
?
CO + dithionite + H+
CH4 + C2H6 + C2H4 + C3H6 + C3H8 + ?
-
no substrate for wild-type
MoFe subunit mutants V70A and V70G will catalyze the reduction and coupling of CO to form methane, ethane, ethylene, propene, and propane. The rates and ratios of hydrocarbon production from CO can be adjusted by changing the flux of electrons through nitrogenase, by substitution of other amino acids located near the FeMo-cofactor, or by changing the partial pressure of CO. Increasing the partial pressure of CO shifts the product ratio in favor of the longer chain alkanes and alkenes
-
?
CO + europium(II) diethylenetriaminepentaacetate + H+

?
-
-
cofactor-deficient enzyme catalyzes formation of methane, ethane, ethene, propane, propene
-
?
CO + europium(II) diethylenetriaminepentaacetate + H+
?
-
-
cofactor-deficient enzyme catalyzes formation of methane, ethane, ethene, propane, propene
-
?
cyanide + ?

?
-
-
-
?
cyanide + ?
?
-
cyanide favors the molydenum for binding
-
-
?
cyanide + ?
?
-
cyanide favors the molydenum for binding
-
-
?
cyclopropene + ?

?
-
-
-
-
?
cyclopropene + ?
?
-
-
-
-
?
diazene + ?

?
-
modified nitrogenase variant V70A/H195Q under turnover conditions using diazene, methyldiazene, or hydrazine as substrate traps a common S = 1/2 intermediate. Such samples also contain a common intermediate with FeMo-co in an integer-spin state having a ground-state non-Kramers doublet. This species, designated H, has NH2 bound to FeMo-co and corresponds to the penultimate intermediate of N2 hydrogenation, the state formed after the accumulation of seven electrons/protons and the release of the first NH3, the S = 1/2 species corresponds to the final intermediate in N2 reduction, the state formed after accumulation of eight electrons/protons, with NH3 still bound to FeMo-co prior to release and regeneration of resting-state FeMo-co
-
-
?
diazene + ?
?
-
modified nitrogenase variant V70A/H195Q under turnover conditions using diazene, methyldiazene, or hydrazine as substrate traps a common S = 1/2 intermediate. Such samples also contain a common intermediate with FeMo-co in an integer-spin state having a ground-state non-Kramers doublet. This species, designated H, has NH2 bound to FeMo-co and corresponds to the penultimate intermediate of N2 hydrogenation, the state formed after the accumulation of seven electrons/protons and the release of the first NH3, the S = 1/2 species corresponds to the final intermediate in N2 reduction, the state formed after accumulation of eight electrons/protons, with NH3 still bound to FeMo-co prior to release and regeneration of resting-state FeMo-co
-
-
?
dithionite + H+ + acetylene + ATP

?
-
-
-
-
?
dithionite + H+ + acetylene + ATP
?
-
-
-
-
?
dithionite + H+ + N2 + ATP

?
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
-
SO2- being the actual nitrogenase reductant, reaction kinetics
-
-
?
dithionite + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
dithionite + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
ethylene + ?

?
-
-
-
-
?
hydrazine + ?

?
-
-
-
-
?
hydrazine + ?
?
-
high activity with the Val70 mutant enzyme, poor substrate for the wild-type enzyme
-
-
?
hydrazine + ?
?
-
-
-
-
?
methyl isocyanide + ?

?
-
-
-
?
methyl isocyanide + ?
?
-
-
-
-
?
methyldiazene + ?

?
-
-
-
-
?
methyldiazene + ?
?
-
-
-
-
?
N2 + 10 H+ + 8 e- + 16 ATP

2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
N2 + 10 H+ + 8 e- + 16 ATP
2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+

2 NH3 + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
-
the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
-
relaxation of the nitrogenase H+/H+ intermediate during step-annealing
-
-
?
N2 + 8 e- + 8 H+ + 16 ATP

2 NH3 + H2 + 16 ADP + 16 phosphate
-
-
-
-
ir
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
-
cofactor binding structure analysis, Fe protein-MoFe protein complex structure in the presence of ATP analogue AMPPCP, overview
-
-
ir
N2O + ?

?
-
-
-
?
N3- + ?

?
-
-
-
?
propargyl alcohol + ?

?
-
wild-type enzyme and V70A mutant MoFe protein-containing enzyme
-
-
?
propargyl alcohol + ?
?
-
wild-type enzyme and V70A mutant MoFe protein-containing enzyme
-
-
?
reduced ferredoxin + H+ + ATP

oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
Gloeocapsa sp.
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
H2-producing activity is much higher in the iron-only enzyme form than in the molybdenum containing form and is less inhibited by competitive substrates
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
H2-producing activity is much higher in the iron-only enzyme form than in the molybdenum containing form and is less inhibited by competitive substrates
-
?
reduced ferredoxin + H+ + ATP
oxidized ferredoxin + H2 + ADP + phosphate
-
in absence of other acceptors
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP

oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
Chromatium sp.
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + CH3NC + ATP
oxidized ferredoxin + CH4 + C2H4 + C3H6 + C3H8 + CH3NH2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP

oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
Chromatium sp.
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + CN- + ATP
oxidized ferredoxin + CH4 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O

oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
enzyme complex is responsible for the majority of biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
in absence of N2 or other substrates, the electron flow is directed towards proton reduction
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
turnover cycle scheme, MgATP is required for activity, mechanism of MgATP hydrolysis and electron transfer with an important role of switch I and II within the Fe protein
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
reduction of atmospheric dinitrogen to ammonium
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2O + ATP

oxidized ferredoxin + H2O + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2O + ATP
oxidized ferredoxin + H2O + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP

oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
mutant H195Q shows only about 7.5% activity compared to wild-type
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
Chromatium sp.
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N3- + ATP
oxidized ferredoxin + NH3 + N2 + ADP + phosphate
-
-
-
?
Ti4+ + H+ + N2 + ATP

?
-
in vitro substrate
-
-
?
Ti4+ + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
Ti4+ + H+ + N2 + ATP
?
-
in vitro substrate
-
-
?
additional information

?
-
-
FeVco is extracted intact, carrying with it the characteristic capacity to reduce C2H2 to C2H6 and, perhaps even more importantly, the ability to reduce N2 to NH3
-
-
?
additional information
?
-
-
FeVco is extracted intact, carrying with it the characteristic capacity to reduce C2H2 to C2H6 and, perhaps even more importantly, the ability to reduce N2 to NH3
-
-
?
additional information
?
-
the activity of the enzyme complex is regulated by specific interactions, inducing conformational changes, between the complex components, overview
-
-
?
additional information
?
-
catalytic role of the molybdenum-iron protein, with P-cluster, and the Fe protein
-
-
?
additional information
?
-
-
nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview
-
-
?
additional information
?
-
-
nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor
-
-
?
additional information
?
-
substrates bind and are reduced at a single 4Fe-4S face of the FeMo-cofactor. When alpha70Val is substituted by alpha70Ile, access of substrates to Fe6 of this face is effectively blocked
-
-
?
additional information
?
-
-
in the draft mechanism model, H2 is produced by reductive elimination of the two bridging hydrides of a four-electron reduced intermediate during N2 binding. This process releases H2, yielding N2 bound to FeMo-cofactor that is doubly reduced relative to the resting redox level, and thereby is activated to promptly generate bound diazene. This mechanism predicts that during turnover under D2/N2, the reverse reaction of D2 with the N2-bound product of reductive elimination would generate a dideutero-four-electron reduced intermediate, which can relax with loss of HD to the state designated two-electron reduced intermediate, with a single deuteride bridge. The predicted two-electron reduced intermediate(D) and four-electron reduced intermediate(2D) states are established by intercepting them with the nonphysiological substrate acetylene to generate deuterated ethylenes. That gaseous H2/D2 can reduce a substrate other than H+ with N2 as a cocatalyst confirms the essential mechanistic role for H2 formation, and hence a limiting stoichiometry for biological nitrogen fixation of eight electrons/protons
-
-
?
additional information
?
-
-
a variant enzym containing P-clusters which consist of paired [Fe4S4]-like clusters, can catalyze ATP-independent substrate reduction in the presence of a strong reductant, europium (II) diethylenetriaminepentaacetate [Eu(II)-DTPA]. The variant P*-cluster is not only capable of catalyzing the two-electron reduction of proton, acetylene, ethylene, and hydrazine, but also capable of reducing cyanide, carbon monoxide, and carbon dioxide to alkanes and alkenes
-
-
?
additional information
?
-
-
data support a deficit-spending model of electron transfer where the first event is electron tranfer from the P-cluster to FeMo-cofactor and the second, backfill, event is fast electron tranfer from the Fe protein [4Fe-4S] cluster to the oxidized P-cluster. The first electron transfer is conformationally gated, whereas the second is not
-
-
?
additional information
?
-
-
draft mechanism for N2 reduction by nitrogenase. Diazene binds to the one-electron reduced intermediate with the release of H2, and enters the N2 pathway as the final form of the four-electron reduced state. In contrast, N2H4 instead binds to one-electron reduced intermediate, as is proposed for another two-electron substrate, C2H2, and joins the N2 pathway at a stage corresponding to the seven-electron reduced intermediate in the N2 reduction scheme
-
-
?
additional information
?
-
-
using buffer 3-(N-morpholino)propanesulfonic acid, which has a very small temperature coefficient, temperature-dependent elctron transfer rate constants are observed, with nonlinear Arrhenius plots and with electron transfers gated across the temperature range by a conformational change that involves the binding of numerous water molecules, consistent with an unchanging electron transfer mechanism. There is no solvent kinetic isotope effect throughout the temperature range studied, consistent with an unchanging mechanismn. The nonlinear Arrhenius plots are explained by the change in heat capacity caused by the binding of water molecules in an invariant gating electron transfer mechanism. The observations contradict the idea of a change in electron transfer mechanism with cooling
-
-
?
additional information
?
-
nitrite and hydroxylamine are nitrogenase substrates. The proposed NO2- reduction intermediate hydroxylamine (NH2OH) is a nitrogenase substrate, reduction intermediates can be trapped, cf. EC 1.7.2.2
-
-
?
additional information
?
-
nitrite and hydroxylamine as nitrogenase substrates. The proposed NO2- reduction intermediate hydroxylamine (NH2OH) is a nitrogenase substrate, reduction intermediates can be trapped, cf. EC 1.7.2.2
-
-
?
additional information
?
-
-
a variant enzym containing P-clusters which consist of paired [Fe4S4]-like clusters, can catalyze ATP-independent substrate reduction in the presence of a strong reductant, europium (II) diethylenetriaminepentaacetate [Eu(II)-DTPA]. The variant P*-cluster is not only capable of catalyzing the two-electron reduction of proton, acetylene, ethylene, and hydrazine, but also capable of reducing cyanide, carbon monoxide, and carbon dioxide to alkanes and alkenes
-
-
?
additional information
?
-
-
draft mechanism for N2 reduction by nitrogenase. Diazene binds to the one-electron reduced intermediate with the release of H2, and enters the N2 pathway as the final form of the four-electron reduced state. In contrast, N2H4 instead binds to one-electron reduced intermediate, as is proposed for another two-electron substrate, C2H2, and joins the N2 pathway at a stage corresponding to the seven-electron reduced intermediate in the N2 reduction scheme
-
-
?
additional information
?
-
-
in the draft mechanism model, H2 is produced by reductive elimination of the two bridging hydrides of a four-electron reduced intermediate during N2 binding. This process releases H2, yielding N2 bound to FeMo-cofactor that is doubly reduced relative to the resting redox level, and thereby is activated to promptly generate bound diazene. This mechanism predicts that during turnover under D2/N2, the reverse reaction of D2 with the N2-bound product of reductive elimination would generate a dideutero-four-electron reduced intermediate, which can relax with loss of HD to the state designated two-electron reduced intermediate, with a single deuteride bridge. The predicted two-electron reduced intermediate(D) and four-electron reduced intermediate(2D) states are established by intercepting them with the nonphysiological substrate acetylene to generate deuterated ethylenes. That gaseous H2/D2 can reduce a substrate other than H+ with N2 as a cocatalyst confirms the essential mechanistic role for H2 formation, and hence a limiting stoichiometry for biological nitrogen fixation of eight electrons/protons
-
-
?
additional information
?
-
-
nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth
-
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes, reduction reactions using acetylene, propyne, 1-butyne, 2-butyne, propargyl alcohol, 2-butyne-1-ol, and 2-butyne-1,4-diol as substrates, overview
-
-
?
additional information
?
-
-
data support a deficit-spending model of electron transfer where the first event is electron tranfer from the P-cluster to FeMo-cofactor and the second, backfill, event is fast electron tranfer from the Fe protein [4Fe-4S] cluster to the oxidized P-cluster. The first electron transfer is conformationally gated, whereas the second is not
-
-
?
additional information
?
-
-
using buffer 3-(N-morpholino)propanesulfonic acid, which has a very small temperature coefficient, temperature-dependent elctron transfer rate constants are observed, with nonlinear Arrhenius plots and with electron transfers gated across the temperature range by a conformational change that involves the binding of numerous water molecules, consistent with an unchanging electron transfer mechanism. There is no solvent kinetic isotope effect throughout the temperature range studied, consistent with an unchanging mechanismn. The nonlinear Arrhenius plots are explained by the change in heat capacity caused by the binding of water molecules in an invariant gating electron transfer mechanism. The observations contradict the idea of a change in electron transfer mechanism with cooling
-
-
?
additional information
?
-
-
influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview
-
-
?
additional information
?
-
-
influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview
-
-
?
additional information
?
-
-
gene nifX and the contigous gene orf1 are essential for maximum nitrogen fixation under iron limitation and are probably involved in synthesis of nitrogenase iron or iron-molybdenum clusters
-
-
?
additional information
?
-
-
substrate reduction specific activities of the recombinant chimeric NifDK/NifBco protein compared to those of wild-type NifDK, effect of molybdenum and homocitrate addition, overview. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3
-
-
?
additional information
?
-
-
substrate reduction specific activities of the recombinant chimeric NifDK/NifBco protein compared to those of wild-type NifDK, effect of molybdenum and homocitrate addition, overview. In contrast to the NifDK protein containing FeMo-cofactor at the active site, NifB-co-containing NifDK is unable to reduce N2 into NH3
-
-
?
additional information
?
-
-
enzyme activity causes acetylene production
-
-
?
additional information
?
-
-
both nifI1 and nifI2 are required for regulation in vivo
-
-
?
additional information
?
-
-
the enzyme performs acetylene reduction
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
hydrazine + reduced ferredoxin
2 NH3 + oxidized ferredoxin
-
-
-
?
hydroxylamine + reduced ferredoxin
NH3 + H2O + oxidized ferredoxin
-
-
-
?
N2 + 10 H+ + 8 e- + 16 ATP
2 NH4+ + H2 + 16 ADP + 16 phosphate
N2 + 4 reduced ferredoxin
hydrazine + 4 oxidized ferredoxin
-
-
-
?
N2 + 8 e- + 16 ATP + 8 H+
2 NH3 + H2 + 16 ADP + 16 phosphate
-
the enzyme is responsible for biological nitrogen fixation, the conversion of atmospheric N2 to NH3
-
-
?
N2 + 8 e- + 8 H+ + 16 ATP
2 NH3 + H2 + 16 ADP + 16 phosphate
-
-
-
-
ir
nitrite + 4 reduced ferredoxin + 5 H+
hydroxylamine + H2O + 4 oxidized ferredoxin
-
-
-
?
nitrite + H+ + ATP + reduced ferredoxin
NH3 + 2 H2O + 12 ADP + 12 phosphate + oxidized ferredoxin
overall reaction
-
-
?
reduced ferredoxin + H+ + N2 + ATP
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
additional information
?
-
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O

2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
-
?
2 reduced ferredoxin + 2 H+ + acetylene + 2 ATP + 2 H2O
2 oxidized ferredoxin + ethylene + 2 ADP + 2 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O

8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
440138, 440142, 440143, 440144, 440145, 440146, 440147, 440150, 440153, 440154, 440155, 440156, 440158, 440163, 440166 -
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
overall reaction
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Chromatium sp.
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Chromatium sp.
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Chromatium sp.
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
440142, 440143, 440144, 440145, 440146, 440147, 440153, 440159, 440164, 440174, 440180 -
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cyanobacterium sp.
-
ferredoxin normally functions as immediate electron donor to nitrogenase, during iron starvation it is replaced by flavodoxin
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cyanobacterium sp.
-
regulation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Cyanobacterium sp.
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
Gloeocapsa sp.
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
440140, 440142, 440143, 440144, 440145, 440146, 440147, 440149, 440152, 440157, 440166 -
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
biological N2 fixation
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
ferredoxin is the immediate electron carrier to nitrogenase in all nitrogen-fixing organisms with the exception of Klebsiella pneumoniae, and possibly Azotobacter species, where only flavodoxin is effective in coupling electron flow to nitrogenase
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
-
?
N2 + 10 H+ + 8 e- + 16 ATP

2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
N2 + 10 H+ + 8 e- + 16 ATP
2 NH4+ + H2 + 16 ADP + 16 phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O

oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
enzyme complex is responsible for the majority of biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
reduction of atmospheric dinitrogen to ammonium
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
biological nitrogen fixation
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
ir
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
reduced ferredoxin + H+ + N2 + ATP + H2O
oxidized ferredoxin + H2 + NH3 + ADP + phosphate
-
-
-
-
?
additional information

?
-
the activity of the enzyme complex is regulated by specific interactions, inducing conformational changes, between the complex components, overview
-
-
?
additional information
?
-
-
nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth
-
-
?
additional information
?
-
-
nitrogenase catalyzes the nucleotide-dependent conversion of dinitrogen to ammonia at the iron-molybdenum cofactor center of its molybdenum-iron protein component. Mo and homocitrate can be loaded onto the Fe protein upon ATP hydrolysis. Mo may enter the Fe protein by attaching to the position that corresponds to the gamma-phosphate of ATP following the hydrolysis of ATP. Subsequently, the loaded Fe protein can deliver Mo and homocitrate to the NifEN-associated precursor and transform the precursor into a fully matured iron-molybdenum cofactor
-
-
?
additional information
?
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in the draft mechanism model, H2 is produced by reductive elimination of the two bridging hydrides of a four-electron reduced intermediate during N2 binding. This process releases H2, yielding N2 bound to FeMo-cofactor that is doubly reduced relative to the resting redox level, and thereby is activated to promptly generate bound diazene. This mechanism predicts that during turnover under D2/N2, the reverse reaction of D2 with the N2-bound product of reductive elimination would generate a dideutero-four-electron reduced intermediate, which can relax with loss of HD to the state designated two-electron reduced intermediate, with a single deuteride bridge. The predicted two-electron reduced intermediate(D) and four-electron reduced intermediate(2D) states are established by intercepting them with the nonphysiological substrate acetylene to generate deuterated ethylenes. That gaseous H2/D2 can reduce a substrate other than H+ with N2 as a cocatalyst confirms the essential mechanistic role for H2 formation, and hence a limiting stoichiometry for biological nitrogen fixation of eight electrons/protons
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nitrite and hydroxylamine are nitrogenase substrates. The proposed NO2- reduction intermediate hydroxylamine (NH2OH) is a nitrogenase substrate, reduction intermediates can be trapped, cf. EC 1.7.2.2
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additional information
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in the draft mechanism model, H2 is produced by reductive elimination of the two bridging hydrides of a four-electron reduced intermediate during N2 binding. This process releases H2, yielding N2 bound to FeMo-cofactor that is doubly reduced relative to the resting redox level, and thereby is activated to promptly generate bound diazene. This mechanism predicts that during turnover under D2/N2, the reverse reaction of D2 with the N2-bound product of reductive elimination would generate a dideutero-four-electron reduced intermediate, which can relax with loss of HD to the state designated two-electron reduced intermediate, with a single deuteride bridge. The predicted two-electron reduced intermediate(D) and four-electron reduced intermediate(2D) states are established by intercepting them with the nonphysiological substrate acetylene to generate deuterated ethylenes. That gaseous H2/D2 can reduce a substrate other than H+ with N2 as a cocatalyst confirms the essential mechanistic role for H2 formation, and hence a limiting stoichiometry for biological nitrogen fixation of eight electrons/protons
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nitrogenase catalyzes the biological reduction of N2 to ammonia as well as the two-electron reduction of the nonphysiological alkyne substrate, alkyne substrate interaction within the nitrogenase MoFe protein, overview, the addition of neither 2-butyne-1-ol nor 2-butyne-1,4-diol to the growth medium has any effect on the capacity of wild-type Azotobacter vinelandii to sustain diazotrophic growth
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influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview
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influence of carbon and nitrogen sources on enzyme activity, amino acids in the apoplastic and symplastic sap of sugarcane stems might have a regulatiry role on growth and nitrogenase activity during symbiotic association, overview
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gene nifX and the contigous gene orf1 are essential for maximum nitrogen fixation under iron limitation and are probably involved in synthesis of nitrogenase iron or iron-molybdenum clusters
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enzyme activity causes acetylene production
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both nifI1 and nifI2 are required for regulation in vivo
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