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dc.citation.endPage 1714 -
dc.citation.number 12 -
dc.citation.startPage 1712 -
dc.citation.title CHEMBIOCHEM -
dc.citation.volume 16 -
dc.contributor.author Schilter, David -
dc.date.accessioned 2023-12-22T00:48:11Z -
dc.date.available 2023-12-22T00:48:11Z -
dc.date.created 2017-09-13 -
dc.date.issued 2015-08 -
dc.description.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. -
dc.identifier.bibliographicCitation CHEMBIOCHEM, v.16, no.12, pp.1712 - 1714 -
dc.identifier.doi 10.1002/cbic.201500270 -
dc.identifier.issn 1439-4227 -
dc.identifier.scopusid 2-s2.0-84938739534 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/22687 -
dc.identifier.url http://onlinelibrary.wiley.com/doi/10.1002/cbic.201500270/abstract -
dc.identifier.wosid 000359314400002 -
dc.language 영어 -
dc.publisher WILEY-V C H VERLAG GMBH -
dc.title Nickel-Iron Hydrogenases: High-Resolution Crystallography Resolves the Hydride, but Not the Debate -
dc.type Article -
dc.description.isOpenAccess FALSE -
dc.relation.journalWebOfScienceCategory Biochemistry & Molecular Biology; Chemistry, Medicinal -
dc.relation.journalResearchArea Biochemistry & Molecular Biology; Pharmacology & Pharmacy -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor biomimetic models -
dc.subject.keywordAuthor enzyme catalysis -
dc.subject.keywordAuthor hydrides -
dc.subject.keywordAuthor hydrogenases -
dc.subject.keywordAuthor X-ray crystallography -
dc.subject.keywordPlus NIFE HYDROGENASE -
dc.subject.keywordPlus DESULFOVIBRIO-GIGAS -
dc.subject.keywordPlus ACTIVE-SITE -
dc.subject.keywordPlus ACTIVATION -
dc.subject.keywordPlus LIGAND -
dc.subject.keywordPlus ENDOR -
dc.subject.keywordPlus MODEL -

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