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Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases

Hydrogen gas obtained from cheap or sustainable sources has been investigated as an alternative to fossil fuels. By using hydrogenase (H(2)ase) and formate dehydrogenase (FDH), H(2) and CO(2) gases can be converted to formate, which can be conveniently stored and transported. However, developing an...

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Autores principales: Cha, Jaehyun, Bak, Hyeonseon, Kwon, Inchan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9849572/
https://www.ncbi.nlm.nih.gov/pubmed/36686231
http://dx.doi.org/10.3389/fbioe.2022.1078164
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author Cha, Jaehyun
Bak, Hyeonseon
Kwon, Inchan
author_facet Cha, Jaehyun
Bak, Hyeonseon
Kwon, Inchan
author_sort Cha, Jaehyun
collection PubMed
description Hydrogen gas obtained from cheap or sustainable sources has been investigated as an alternative to fossil fuels. By using hydrogenase (H(2)ase) and formate dehydrogenase (FDH), H(2) and CO(2) gases can be converted to formate, which can be conveniently stored and transported. However, developing an enzymatic process that converts H(2) and CO(2) obtained from cheap sources into formate is challenging because even a very small amount of O(2) included in the cheap sources damages most H(2)ases and FDHs. In order to overcome this limitation, we investigated a pair of oxygen-tolerant H(2)ase and FDH. We achieved the cascade reaction between H(2)ase from Ralstonia eutropha H16 (ReSH) and FDH from Rhodobacter capsulatus (RcFDH) to convert H(2) and CO(2) to formate using in situ regeneration of NAD(+)/NADH in the presence of O(2).
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spelling pubmed-98495722023-01-20 Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases Cha, Jaehyun Bak, Hyeonseon Kwon, Inchan Front Bioeng Biotechnol Bioengineering and Biotechnology Hydrogen gas obtained from cheap or sustainable sources has been investigated as an alternative to fossil fuels. By using hydrogenase (H(2)ase) and formate dehydrogenase (FDH), H(2) and CO(2) gases can be converted to formate, which can be conveniently stored and transported. However, developing an enzymatic process that converts H(2) and CO(2) obtained from cheap sources into formate is challenging because even a very small amount of O(2) included in the cheap sources damages most H(2)ases and FDHs. In order to overcome this limitation, we investigated a pair of oxygen-tolerant H(2)ase and FDH. We achieved the cascade reaction between H(2)ase from Ralstonia eutropha H16 (ReSH) and FDH from Rhodobacter capsulatus (RcFDH) to convert H(2) and CO(2) to formate using in situ regeneration of NAD(+)/NADH in the presence of O(2). Frontiers Media S.A. 2023-01-05 /pmc/articles/PMC9849572/ /pubmed/36686231 http://dx.doi.org/10.3389/fbioe.2022.1078164 Text en Copyright © 2023 Cha, Bak and Kwon. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Bioengineering and Biotechnology
Cha, Jaehyun
Bak, Hyeonseon
Kwon, Inchan
Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases
title Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases
title_full Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases
title_fullStr Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases
title_full_unstemmed Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases
title_short Hydrogen-fueled CO(2) reduction using oxygen-tolerant oxidoreductases
title_sort hydrogen-fueled co(2) reduction using oxygen-tolerant oxidoreductases
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9849572/
https://www.ncbi.nlm.nih.gov/pubmed/36686231
http://dx.doi.org/10.3389/fbioe.2022.1078164
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