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Q34469478-224FA9E1-8F25-451F-92D8-F2A0A0E7DEA8
Q34469478-224FA9E1-8F25-451F-92D8-F2A0A0E7DEA8
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http://www.wikidata.org/entity/statement/Q34469478-224FA9E1-8F25-451F-92D8-F2A0A0E7DEA8
Site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in CaHydA [FeFe]-hydrogenase.
P2860
Q34469478-224FA9E1-8F25-451F-92D8-F2A0A0E7DEA8
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34469478-224FA9E1-8F25-451F-92D8-F2A0A0E7DEA8
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wasDerivedFrom
c4a733036fa7139d45c25f83e95beaee3fba2db3
P2860
Electrochemical kinetic investigations of the reactions of [FeFe]-hydrogenases with carbon monoxide and oxygen: comparing the importance of gas tunnels and active-site electronic/redox effects.