Direct electron transfer between frhAGB-encoding hydrogenase and TrxR in a non-methanogenic hyperthermophilic archaeon

DC Field Value Language
dc.contributor.author 정해창 -
dc.contributor.author 임재규 -
dc.contributor.author 이현숙 -
dc.contributor.author 강성균 -
dc.date.accessioned 2020-07-15T11:33:26Z -
dc.date.available 2020-07-15T11:33:26Z -
dc.date.created 2020-02-11 -
dc.date.issued 2018-07-30 -
dc.identifier.uri https://sciwatch.kiost.ac.kr/handle/2020.kiost/23178 -
dc.description.abstract Previously, a gene cluster homologous to the frhAGB encoding F420-reducing hydrogenase (Frh) was identified in a non-methanogen Thermococcus onnurineus NA.The heterotrimeric enzyme complex exhibited hydrogenase activity with methyl viologen, FMN or FAD as electron acceptor, but not with deazaflavin coenzyme F420, implicating that it has a role distinct from that of homologues from methanogens. Herein, we describe that Frh from T. onnurineus NA1 can reduce thioredoxin reductase (TrxR). In the course of understanding the role of TrxR in T. onnurineus NA1, we employed protein-protein interaction tools and some protein bands, of which one band was identified as a protein coded by frhG afterwards, were pulled down with TrxR in the immunoprecipitation experiment using an antibody against TrxR. The relationship between the hydrogenase and TrxR was further investigated, and TrxR could be reduced directly by Frh, coupled with H2 oxidation in the absence of any other electron carriers. Subsequently, the reduced TrxR by Frh relayed cascade of electron transfer to a sulfur response regulator, SurR. The mechanism behind the phenomena will be discussed., FMN or FAD as electron acceptor, but not with deazaflavin coenzyme F420, implicating that it has a role distinct from that of homologues from methanogens. Herein, we describe that Frh from T. onnurineus NA1 can reduce thioredoxin reductase (TrxR). In the course of understanding the role of TrxR in T. onnurineus NA1, we employed protein-protein interaction tools and some protein bands, of which one band was identified as a protein coded by frhG afterwards, were pulled down with TrxR in the immunoprecipitation experiment using an antibody against TrxR. The relationship between the hydrogenase and TrxR was further investigated, and TrxR could be reduced directly by Frh, coupled with H2 oxidation in the absence of any other electron carriers. Subsequently, the reduced TrxR by Frh relayed cascade of electron transfer to a sulfur response regulator, SurR. The mechanism behind the phenomena will be discussed. -
dc.description.uri 1 -
dc.language English -
dc.publisher Gordon Research Conference -
dc.relation.isPartOf gordon research conferences/ Molecular Basis of Microbial One-Carbon Metabolism -
dc.title Direct electron transfer between frhAGB-encoding hydrogenase and TrxR in a non-methanogenic hyperthermophilic archaeon -
dc.type Conference -
dc.citation.conferencePlace US -
dc.citation.title gordon research conferences/ Molecular Basis of Microbial One-Carbon Metabolism -
dc.identifier.bibliographicCitation gordon research conferences/ Molecular Basis of Microbial One-Carbon Metabolism -
dc.description.journalClass 1 -
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Marine Resources Research Division > Marine Biotechnology Research Center > 2. Conference Papers
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