Literature summary extracted from
Lee, C.C.; Hu, Y.; Ribbe, M.W.
Vanadium nitrogenase reduces CO (2010), Science, 329, 642.
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 |