Literature summary for 1.12.99.6 extracted from

Finkelmann, A.R.; Stiebritz, M.T.; Reiher, M.
Kinetic modeling of hydrogen conversion at [Fe] hydrogenase active-site models (2013), J. Phys. Chem. B, 117, 4806-4817.

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Organism

Organism	UniProt	Comment	Textmining
synthetic construct	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	study on the catalytic mechanism of an active-site model of [Fe] hydrogenase by small modifications of the first ligand shell. Dispersion interactions between the active site and the hydride acceptor methenyltetrahydromethanopterin render the hydride transfer step less endergonic and lower its barrier. Substitution of CO by CN-, which resembles [FeFe] hydrogenase-like coordination, inverts the elementary steps H- transfer and H2 cleavage. The catalytic efficiency of [Fe] hydrogenase can be attributed to a flat energy profile throughout the catalytic cycle. Intermediates that are too stable, as they occur, e.g., when one CO ligand is substituted by CN-, significantly slow down the turnover rate of the enzyme. The catalytic activity of the wild-type form of the active-site model could, however, be enhanced by a PH3 ligand substitution of the CO ligand	synthetic construct	?	-	?

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Release 2023.1 (January 2023)