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Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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dc.citation.startPage 539 -
dc.citation.title COMMUNICATIONS BIOLOGY -
dc.citation.volume 5 - Lim, Jae Kyu - Yang, Ji-In - Kim, Yun Jae - Park, Yeong-Jun - Kim, Yong Hwan - 2023-12-21T14:08:36Z - 2023-12-21T14:08:36Z - 2022-06-10 - 2022-06 -
dc.description.abstract Ferredoxin-dependent metabolic engineering of electron transfer circuits has been developed to enhance redox efficiency in the field of synthetic biology, e.g., for hydrogen production and for reduction of flavoproteins or NAD(P)+. Here, we present the bioconversion of carbon monoxide (CO) gas to formate via a synthetic CO:formate oxidoreductase (CFOR), designed as an enzyme complex for direct electron transfer between non-interacting CO dehydrogenase and formate dehydrogenase using an electron-transferring Fe-S fusion protein. The CFOR-introduced Thermococcus onnurineus mutant strains showed CO-dependent formate production in vivo and in vitro. The maximum formate production rate from purified CFOR complex and specific formate productivity from the bioreactor were 2.2 ± 0.2 μmol/mg/min and 73.1 ± 29.0 mmol/g-cells/h, respectively. The CO-dependent CO2 reduction/formate production activity of synthetic CFOR was confirmed, indicating that direct electron transfer between two unrelated dehydrogenases was feasible via mediation of the FeS-FeS fusion protein. -
dc.identifier.bibliographicCitation COMMUNICATIONS BIOLOGY, v.5, pp.539 -
dc.identifier.doi 10.1038/s42003-022-03513-7 -
dc.identifier.issn 2399-3642 -
dc.identifier.scopusid 2-s2.0-85131181547 -
dc.identifier.uri -
dc.identifier.url -
dc.identifier.wosid 000805809700004 -
dc.language 영어 -
dc.publisher NATURE RESEARCH -
dc.title Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea -
dc.type Article -
dc.description.isOpenAccess TRUE -
dc.relation.journalWebOfScienceCategory Biology;Multidisciplinary Sciences -
dc.relation.journalResearchArea Life Sciences & Biomedicine - Other TopicsScience & Technology - Other Topics; -
dc.type.docType Article -
dc.description.journalRegisteredClass scie -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus THERMOCOCCUS-ONNURINEUS NA1 -
dc.subject.keywordPlus IRON-SULFUR PROTEIN -
dc.subject.keywordPlus DEPENDENT H-2 PRODUCTION -
dc.subject.keywordPlus CRYSTAL-STRUCTURE -
dc.subject.keywordPlus FUSION PROTEIN -
dc.subject.keywordPlus DEHYDROGENASE -
dc.subject.keywordPlus PURIFICATION -
dc.subject.keywordPlus REDUCTASE -
dc.subject.keywordPlus REVEALS -
dc.subject.keywordPlus CONSTRUCTION -


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