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Q34469478-493C813F-83B7-4D31-B70E-167BB5DD01AF
Q34469478-493C813F-83B7-4D31-B70E-167BB5DD01AF
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34469478-493C813F-83B7-4D31-B70E-167BB5DD01AF
Site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in CaHydA [FeFe]-hydrogenase.
P2860
Q34469478-493C813F-83B7-4D31-B70E-167BB5DD01AF
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34469478-493C813F-83B7-4D31-B70E-167BB5DD01AF
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wasDerivedFrom
c4a733036fa7139d45c25f83e95beaee3fba2db3
P2860
The quest for a functional substrate access tunnel in FeFe hydrogenase.