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Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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dc.citation.startPage 130248 -
dc.citation.title BIORESOURCE TECHNOLOGY -
dc.citation.volume 394 - Kim, Suk Min - Kang, Sung Heuck - Jeon, Byong Wook - Kim, Yong Hwan - 2023-12-30T15:35:09Z - 2023-12-30T15:35:09Z - 2023-12-30 - 2024-02 -
dc.description.abstract Carbon monoxide dehydrogenase (CODH), formate dehydrogenase (FDH), hydrogenase (H2ase), and nitrogenase (N2ase) are crucial enzymatic catalysts that facilitate the conversion of industrially significant gases such as CO, CO2, H2, and N2. The tunnels in the gas-converting enzymes serve as conduits for these low molecular weight gases to access deeply buried catalytic sites. The identification of the substrate tunnels is imperative for comprehending the substrate selectivity mechanism underlying these gas-converting enzymes. This knowledge also holds substantial value for industrial applications, particularly in addressing the challenges associated with separation and utilization of byproduct gases. In this comprehensive review, we delve into the emerging field of tunnel engineering, presenting a range of approaches and analyses. Additionally, we propose methodologies for the systematic design of enzymes, with the ultimate goal of advancing protein engineering strategies. -
dc.identifier.bibliographicCitation BIORESOURCE TECHNOLOGY, v.394, pp.130248 -
dc.identifier.doi 10.1016/j.biortech.2023.130248 -
dc.identifier.issn 0960-8524 -
dc.identifier.scopusid 2-s2.0-85181145610 -
dc.identifier.uri -
dc.identifier.wosid 001165663600001 -
dc.language 영어 -
dc.publisher Elsevier BV -
dc.title Tunnel engineering of gas-converting enzymes for inhibitor retardation and substrate acceleration -
dc.type Article -
dc.description.isOpenAccess TRUE -
dc.relation.journalWebOfScienceCategory Agricultural Engineering;Biotechnology & Applied Microbiology;Energy & Fuels -
dc.relation.journalResearchArea Agriculture;Biotechnology & Applied Microbiology;Energy & Fuels -
dc.type.docType Review -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus MOLECULAR-DYNAMICS -
dc.subject.keywordPlus ACTIVE-SITE -
dc.subject.keywordPlus HYDROPHOBIC TUNNEL -
dc.subject.keywordPlus CO DEHYDROGENASE -
dc.subject.keywordPlus PROTEIN -
dc.subject.keywordPlus EFFICIENT -
dc.subject.keywordPlus CHANNEL -
dc.subject.keywordPlus WATER -
dc.subject.keywordPlus TRACKING -
dc.subject.keywordPlus BINDING -


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