Direct Electron Transfer between the frhAGB-Encoded Hydrogenase and Thioredoxin Reductase in the Nonmethanogenic Archaeon Thermococcus onnurineus NA1 SCIE SCOPUS
DC Field | Value | Language |
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dc.contributor.author | Jung, Hae-Chang | - |
dc.contributor.author | Lim, Jae Kyu | - |
dc.contributor.author | Yang, Tae-Jun | - |
dc.contributor.author | Kang, Sung Gyun | - |
dc.contributor.author | Lee, Hyun Sook | - |
dc.date.accessioned | 2020-12-10T07:54:44Z | - |
dc.date.available | 2020-12-10T07:54:44Z | - |
dc.date.created | 2020-05-08 | - |
dc.date.issued | 2020-03 | - |
dc.identifier.issn | 0099-2240 | - |
dc.identifier.uri | https://sciwatch.kiost.ac.kr/handle/2020.kiost/38730 | - |
dc.description.abstract | To date, NAD(P)H, ferredoxin, and coenzyme F-420 have been identified as electron donors for thioredoxin reductase (TrxR). In this study, we present a novel electron source for TrxR. In the hyperthermophilic archaeon Thermococcus onnurineus NA1, the frhAGB-encoded hydrogenase, a homolog of the F-420- reducing hydrogenase of methanogens, was demonstrated to interact with TrxR in coimmuno-precipitation experiments and in vitro pulldown assays. Electrons derived from H-2 oxidation by the frhAGB-encoded hydrogenase were transferred to TrxR and reduced Pdo, a redox partner of TrxR. Interaction and electron transfer were observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR was 7-fold less efficient than when NADPH was the electron donor. This study not only presents a different type of electron donor for TrxR but also reveals new functionality of the frhAGB-encoded hydrogenase utilizing a protein as an electron acceptor. IMPORTANCE This study has importance in that TrxR can use H-2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NAD(P)H in T. onnurineus NA1. Further studies are needed to explore the physiological significance of this protein. This study also has importance as a significant step toward understanding the functionality of the frhAGB-encoded hydrogenase in a nonmethanogen; the hydrogenase can transfer electrons derived from oxidation of H-2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologs, F-420-reducing hydrogenases of methanogens. | - |
dc.description.uri | 1 | - |
dc.language | English | - |
dc.publisher | AMER SOC MICROBIOLOGY | - |
dc.title | Direct Electron Transfer between the frhAGB-Encoded Hydrogenase and Thioredoxin Reductase in the Nonmethanogenic Archaeon Thermococcus onnurineus NA1 | - |
dc.type | Article | - |
dc.citation.title | APPLIED AND ENVIRONMENTAL MICROBIOLOGY | - |
dc.citation.volume | 86 | - |
dc.citation.number | 6 | - |
dc.contributor.alternativeName | 정해창 | - |
dc.contributor.alternativeName | 임재규 | - |
dc.contributor.alternativeName | 양태준 | - |
dc.contributor.alternativeName | 강성균 | - |
dc.contributor.alternativeName | 이현숙 | - |
dc.identifier.bibliographicCitation | APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.86, no.6 | - |
dc.identifier.doi | 10.1128/AEM.02630-19 | - |
dc.identifier.scopusid | 2-s2.0-85081121342 | - |
dc.identifier.wosid | 000522978600017 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.subject.keywordPlus | H-2 PRODUCTION | - |
dc.subject.keywordPlus | SULFUR METABOLISM | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | NICKEL | - |
dc.subject.keywordPlus | SURR | - |
dc.subject.keywordAuthor | F-420-reducing hydrogenase | - |
dc.subject.keywordAuthor | thioredoxin reductase | - |
dc.subject.keywordAuthor | direct electron transfer | - |
dc.subject.keywordAuthor | frhAGB-encoded hydrogenase | - |
dc.subject.keywordAuthor | protein-protein interaction | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |