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Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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dc.citation.endPage 817 -
dc.citation.startPage 807 -
dc.citation.title NATURE CATALYSIS -
dc.citation.volume 5 - Kim, Suk Min - Lee, Jinhee - Kang, Sung Heuck - Heo, Yoonyoung - Yoon, Hye-Jin - Hahn, Ji-Sook - Lee, Hyung Ho - Kim, Yong Hwan - 2023-12-21T13:41:26Z - 2023-12-21T13:41:26Z - 2022-09-21 - 2022-09 -
dc.description.abstract Ni–Fe carbon monoxide dehydrogenases (CODHs) are nearly diffusion-limited biocatalysts that oxidize CO. Their O2 sensitivity, however, is a major drawback for industrial applications. Here we compare the structures of a fast CODH with a high O2 sensitivity (ChCODH-II) and a slower CODH with a lower O2 sensitivity (ChCODH-IV) (Ch, Carboxydothermus hydrogenoformans). Some variants obtained by simple point mutations of the bottleneck residue (A559) in the gas tunnel showed 61–148-fold decreases in O2 sensitivity while maintaining high turnover rates. The variant structure A559W showed obstruction of one gas tunnel, and molecular dynamics supported the locked position of the mutated side chain in the tunnel. The variant was exposed to different gas mixtures, from simple synthetic gas to sophisticated real flue from a steel mill. Its catalytic properties remained unchanged, even at high O2 levels, and the efficiency was maintained for multiple cycles of CO detoxification/regeneration. -
dc.identifier.bibliographicCitation NATURE CATALYSIS, v.5, pp.807 - 817 -
dc.identifier.doi 10.1038/s41929-022-00834-y -
dc.identifier.issn 2520-1158 -
dc.identifier.scopusid 2-s2.0-85137854127 -
dc.identifier.uri -
dc.identifier.wosid 000852936800002 -
dc.language 영어 -
dc.title O2-tolerant CO dehydrogenase via tunnel redesign for the removal of CO from industrial flue gas -
dc.type Article -
dc.description.isOpenAccess TRUE -
dc.relation.journalWebOfScienceCategory Chemistry, Physical -
dc.relation.journalResearchArea Chemistry -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus X-RAY CRYSTALLOGRAPHY -
dc.subject.keywordPlus MOLECULAR-DYNAMICS -
dc.subject.keywordPlus ACTIVE-SITE -
dc.subject.keywordPlus INHIBITION -
dc.subject.keywordPlus LIFE -


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