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Literature summary extracted from

  • Barton, B.E.; Rauchfuss, T.B.
    Terminal hydride in [FeFe]-hydrogenase model has lower potential for H2 production than the isomeric bridging hydride (2008), Inorg. Chem., 47, 2261-2263.
    View publication on PubMedView publication on EuropePMC

Inhibitors

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
1.12.99.6 synthetic construct
-
-
-

Substrates and Products (Substrate)

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
-
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Synonyms

EC Number Synonyms Comment Organism
1.12.99.6 [FeFe]-hydrogenase
-
synthetic construct