Literature summary for 1.12.99.6 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.

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Inhibitors

Inhibitors	Comment	Organism	Structure
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

Metals/Ions	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
synthetic construct	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
H2 + oxidized electron acceptor	-	synthetic construct	H+ + reduced electron acceptor	-	?

Synonyms

Synonyms	Comment	Organism
[FeFe]-hydrogenase	-	synthetic construct

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Release 2023.1 (January 2023)