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Q34469478-19056FD8-6248-4EA8-BEF9-E35B6192A3D7
Q34469478-19056FD8-6248-4EA8-BEF9-E35B6192A3D7
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34469478-19056FD8-6248-4EA8-BEF9-E35B6192A3D7
Site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in CaHydA [FeFe]-hydrogenase.
P2860
Q34469478-19056FD8-6248-4EA8-BEF9-E35B6192A3D7
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34469478-19056FD8-6248-4EA8-BEF9-E35B6192A3D7
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wasDerivedFrom
c4a733036fa7139d45c25f83e95beaee3fba2db3
P2860
Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design.