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Kim, Yong Hwan
School of Energy and Chemical Engineering
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  • 바이오촉매 생물 전환 생물환경

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Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea

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dc.contributor.author Lim, Jae Kyu ko
dc.contributor.author Yang, Ji-In ko
dc.contributor.author Kim, Yun Jae ko
dc.contributor.author Park, Yeong-Jun ko
dc.contributor.author Kim, Yong Hwan ko
dc.date.available 2022-06-17T01:23:38Z -
dc.date.created 2022-06-10 ko
dc.date.issued 2022-06 ko
dc.identifier.citation COMMUNICATIONS BIOLOGY, v.5, pp.539 ko
dc.identifier.issn 2399-3642 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/58670 -
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. ko
dc.language 영어 ko
dc.publisher Nature Publishing Group ko
dc.title Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea ko
dc.type ARTICLE ko
dc.type.rims ART ko
dc.identifier.doi 10.1038/s42003-022-03513-7 ko
dc.identifier.url https://www.nature.com/articles/s42003-022-03513-7 ko
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