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Literature summary for 1.12.99.6 extracted from

  • Abou Hamdan, A.; Dementin, S.; Liebgott, P.P.; Gutierrez-Sanz, O.; Richaud, P.; De Lacey, A.L.; Rousset, M.; Bertrand, P.; Cournac, L.; Leger, C.
    Understanding and tuning the catalytic bias of hydrogenase (2012), J. Am. Chem. Soc., 134, 8368-8371.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
V74C moderate increase in the Michaelis constant for H2. The mutant has the same oxidation activity as the wild-type whereas its maximal H2 production rate varies by 2 orders of magnitude Solidesulfovibrio fructosivorans
V74I moderate increase in the Michaelis constant for H2 Solidesulfovibrio fructosivorans
V74M moderate increase in the Michaelis constant for H2, The mutant has the same oxidation activity as the wild-type whereas its maximal H2 production rate varies by 2 orders of magnitude. The ratio of maximal rates for oxidation over production ranges from 2.5 for the wild-type to 200 for the V74M mutant Solidesulfovibrio fructosivorans

Organism

Organism UniProt Comment Textmining
Solidesulfovibrio fructosivorans
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + methyl viologen
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Solidesulfovibrio fructosivorans H+ + reduced methyl viologen
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?
additional information the catalytic bias, i.e. the ratio of maximal rates in the two directions is not mainly determined by redox properties of the active site, but rather by steps which occur on sites of the proteins that are remote from the active site Solidesulfovibrio fructosivorans ?
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?

Synonyms

Synonyms Comment Organism
NiFe hydrogenase
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Solidesulfovibrio fructosivorans