Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.18.6.1 extracted from

  • Lee, C.C.; Hu, Y.; Ribbe, M.W.
    Vanadium nitrogenase reduces CO (2010), Science, 329, 642.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Iron in the MoFe protein and the Fe protein Azotobacter vinelandii
Molybdenum in the MoFe protein Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
contains nif-encoded molybdenum nitrogenase and vnf-encoded V nitrogenase
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
rates of ATP hydrolysis by Mo and V nitrogenases are comparable under CO, which reflected a similar flux of electrons through the two nitrogenases Azotobacter vinelandii

Synonyms

Synonyms Comment Organism
vanadium nitrogenase
-
Azotobacter vinelandii

Cofactor

Cofactor Comment Organism Structure
ATP
-
Azotobacter vinelandii

General Information

General Information Comment Organism
evolution the ability of V nitrogenase to catalyze both CO and N2 reductions suggests a potential link between the evolution of carbon and nitrogen cycles Azotobacter vinelandii
additional information like the nif-encoded molybdenum nitrogenase, the vnf-encoded V nitrogenase is composed of a specific reductant and a catalytic component. Both nitrogenases use a catalytic mechanism that involves ATP-dependent electron transfer from a reductant, the nifH- or vnfH-encoded Fe protein, to the catalytic component, i.e. nifDK-encoded MoFe protein or vnfDGK-encoded VFe protein, and the reduction of N2 at the cofactor site, i.e. FeMoco or FeVco, of the latter Azotobacter vinelandii
physiological function the diminished H2 evolution by V nitrogenase originates from the diversion of electrons toward CO reduction, in contrast to the Mo nitrogenase Azotobacter vinelandii