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Literature summary 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

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

Organism

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.18.6.1 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

EC Number Synonyms Comment Organism
1.18.6.1 vanadium nitrogenase
-
Azotobacter vinelandii

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 ATP
-
Azotobacter vinelandii

General Information

EC Number General Information Comment Organism
1.18.6.1 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
1.18.6.1 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
1.18.6.1 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