Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | in the MoFe protein and the Fe protein | Azotobacter vinelandii | |
Molybdenum | in the MoFe protein | Azotobacter vinelandii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Azotobacter vinelandii | - |
contains nif-encoded molybdenum nitrogenase and vnf-encoded V nitrogenase | - |
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 | Comment | Organism |
---|---|---|
vanadium nitrogenase | - |
Azotobacter vinelandii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Azotobacter vinelandii |
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 |