Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
about
Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases.Vibrational spectroscopy reveals the initial steps of biological hydrogen evolution.Mechanism of O2 diffusion and reduction in FeFe hydrogenases.[FeFe]-Hydrogenase with Chalcogenide Substitutions at the H-Cluster Maintains Full H2 Evolution Activity.Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
P2860
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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name
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
@ast
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
@en
type
label
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
@ast
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
@en
prefLabel
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
@ast
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.
@en
P2093
P2860
P356
P1433
P1476
Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation
@en
P2093
Kathrin Klein
Martin Winkler
Michael Haumann
Ramona Kositzki
P2860
P2888
P356
10.1038/SREP13978
P407
P50
P577
2015-09-14T00:00:00Z