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Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea

Author(s)
Lim, Jae KyuYang, Ji-InKim, Yun JaePark, Yeong-JunKim, Yong Hwan
Issued Date
2022-06
DOI
10.1038/s42003-022-03513-7
URI
https://scholarworks.unist.ac.kr/handle/201301/58670
Fulltext
https://www.nature.com/articles/s42003-022-03513-7
Citation
COMMUNICATIONS BIOLOGY, v.5, pp.539
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.
Publisher
NATURE RESEARCH
ISSN
2399-3642
Keyword
THERMOCOCCUS-ONNURINEUS NA1IRON-SULFUR PROTEINDEPENDENT H-2 PRODUCTIONCRYSTAL-STRUCTUREFUSION PROTEINDEHYDROGENASEPURIFICATIONREDUCTASEREVEALSCONSTRUCTION

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