Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea
SCIE
SCOPUS
Cited 1 time in
WEB OF SCIENCE
Cited 3 time in
Scopus
-
Title
- Bioconversion of CO to formate by artificially designed carbon monoxide:formate oxidoreductase in hyperthermophilic archaea
-
Author(s)
- Lim, Jae Kyu; Yang, Ji In; Kim, Yun Jae; Park, Yeong Jun; Kim, Yong Hwan
- KIOST Author(s)
- Lim, Jae Kyu(임재규); Yang, Ji In(양지인); Kim, Yun Jae(김윤재); Park, Yeong Jun(박영준)
-
Alternative Author(s)
- 임재규; 양지인; 김윤재; 박영준
-
Publication Year
- 2022-06
-
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 mu mol/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. Synthetic carbon monoxide:formate oxidoreductase is designed for direct electron transfer between non-interacting CO dehydrogenase and formate dehydrogenase using an electron-transferring Fe-S fusion protein in T. onnurineus.
-
ISSN
- 2399-3642
-
URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/42782
-
DOI
- 10.1038/s42003-022-03513-7
-
Bibliographic Citation
- Communications Biology, v.5, no.1, 2022
-
Publisher
- Nature Publishing Group
-
Type
- Article
-
Language
- English
-
Document Type
- Article
- Files in This Item:
-
There are no files associated with this item.
Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.