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Nickel-Iron Hydrogenases: High-Resolution Crystallography Resolves the Hydride, but Not the Debate

Author(s)
Schilter, David
Issued Date
2015-08
DOI
10.1002/cbic.201500270
URI
https://scholarworks.unist.ac.kr/handle/201301/22687
Fulltext
http://onlinelibrary.wiley.com/doi/10.1002/cbic.201500270/abstract
Citation
CHEMBIOCHEM, v.16, no.12, pp.1712 - 1714
Abstract
An (X-ray) eye for detail: Modern high-resolution protein crystallography allows H atoms to be located. Applied to nickel-iron hydrogenase, X-ray structural analysis has finally confirmed the presence of an active-site hydride and thiol, as well as unveiling the intricate pathways that protons take to and from the active site.
Publisher
WILEY-V C H VERLAG GMBH
ISSN
1439-4227
Keyword (Author)
biomimetic modelsenzyme catalysishydrideshydrogenasesX-ray crystallography
Keyword
NIFE HYDROGENASEDESULFOVIBRIO-GIGASACTIVE-SITEACTIVATIONLIGANDENDORMODEL

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