EC Number | Cloned (Comment) | Organism |
---|---|---|
1.18.6.1 | - |
Azotobacter vinelandii |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.18.6.1 | DELTAC153 | mutation in the MoFe protein of nitrogenase. The rate of oxidation of Fe-protein F1+ to this MoFe protein variant is unchanged from the rate to the wild-type MoFe protein, providing further evidence against a gated hopping electron tansfer model | Azotobacter vinelandii |
1.18.6.1 | S188C | mutation in the MoFe protein of nitrogenase. Electron transfer to the MoFe state that contains P-cluster PN and FeMo-cofactor MN is conformationally gated in both wild-type MoFe and S188C mutant MoFe protein and the amino acid substitution S188C does not alter the conformational gate | Azotobacter vinelandii |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.18.6.1 | Azotobacter vinelandii | - |
- |
- |
1.18.6.1 | Azotobacter vinelandii DJ995 | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.6.1 | 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 | Azotobacter vinelandii | ? | - |
? | |
1.18.6.1 | 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 | Azotobacter vinelandii DJ995 | ? | - |
? |