EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.12.99.6 | additional information | isomerization of the terminal hydride is inhibited both by the basicity of the Fe2 complex as well as by the steric size of the dithiolate in the models. In the enzyme, terminal-bridge isomerization may also be inhibited by hydrogen bonding between CNdistal and a epsilon-ammonium center of a nearby, highly conserved lysine residue | synthetic construct |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.12.99.6 | Fe | protonation of diiron dithiolato complexes can occur at a single Fe site, even for symmetrical (FeI)2 compounds. The terminal hydride [HFe2(S2C3H6)(CO)2(dppv)2]+ catalyzes proton reduction at potentials 200 mV milder than the isomeric bridging hydride, thereby establishing a thermodynamic advantage for catalysis operating via terminal hydride | synthetic construct |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.12.99.6 | synthetic construct | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.12.99.6 | H2 + oxidized electron acceptor | - |
synthetic construct | H+ + reduced electron acceptor | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.12.99.6 | [FeFe]-hydrogenase | - |
synthetic construct |