ArticleExtremophiles : life under extreme conditions2015
Characterization of the frhAGB-encoding hydrogenase from a non-methanogenic hyperthermophilic archaeon.
Article in Extremophiles : life under extreme conditions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 15 citations in OpenAlex.
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- NADPApplied and environmental microbiology · 2023Article
- The Piezo-Hyperthermophilic ArchaeonFrontiers in microbiology · 2021Article
- Direct Electron Transfer between theApplied and environmental microbiology · 2020Article
- Biohydrogen production of obligate anaerobic archaeonBiotechnology for biofuels · 2019Article
- Adaptive evolution of a hyperthermophilic archaeon pinpoints a formate transporter as a critical factor for the growth enhancement on formate.Scientific reports · 2017Article
- Article
- Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions.Microbiology and molecular biology reviews : MMBR · 2016Review
- Complete Genome Sequence of the Hyperthermophilic and Piezophilic Archaeon Thermococcus barophilus Ch5, Capable of Growth at the Expense of Hydrogenogenesis from Carbon Monoxide and Formate.Genome announcements · 2016Article
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11 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The F420-reducing hydrogenase has been known as a key enzyme in methanogenesis. Its homologs have been identified in non-methanogenic hyperthermophilic archaea, including Thermococcus onnurineus NA1, but neither physiological function nor biochemical properties have been reported to date. The enzyme of T. onnurineus NA1 was distinguished from those of other methanogens and the members of the family Desulfurobacteriaceae with respect to the phylogenetic distribution of the α and β subunits, organization of frhAGB genes and conservation of F420-coordinating residues. RT-qPCR and Western blot analyses revealed frhA gene is not silent but is expressed in T. onnurineus NA1 grown in the presence of sulfur, carbon monoxide, or formate. The trimeric enzyme complex was purified to homogeneity via affinity chromatography from T. onnurineus NA1 and exhibited catalytic activity toward the electron acceptors such as viologens and flavins but not the deazaflavin coenzyme F420. This is the first biochemical study on the function of the frhAGB-encoding enzyme from a non-methanogenic archaea.
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