ArticleThe Journal of biological chemistry2014
Intact functional fourteen-subunit respiratory membrane-bound [NiFe]-hydrogenase complex of the hyperthermophilic archaeon Pyrococcus furiosus.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- HApplied microbiology and biotechnology · 2026Article
- Mechanistic Principles of Hydrogen Evolution in the Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2024Article
- Harnessing Fermentation May Enhance the Performance of Biological Sulfate-Reducing Bioreactors.Environmental science & technology · 2024Article
- Semi-rational engineering membrane binding domain of L-amino acid deaminase fromFrontiers in microbiology · 2022Article
- Functional Dynamics of an Ancient Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2021Article
- Electron inventory of the iron-sulfur scaffold complex HypCD essential in [NiFe]-hydrogenase cofactor assembly.The Biochemical journal · 2021Article
- Structure of the respiratory MBS complex reveals iron-sulfur cluster catalyzed sulfane sulfur reduction in ancient life.Nature communications · 2020Article
- Article
- Energy-converting hydrogenases: the link between HCellular and molecular life sciences : CMLS · 2020Review
- Formate Is Required for Growth of the Thermophilic Acetogenic BacteriumFrontiers in microbiology · 2020Article
- Inactivation of the uptake hydrogenase in the purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS enables a biological water-gas shift platform for HJournal of industrial microbiology & biotechnology · 2019Article
- Expansive microbial metabolic versatility and biodiversity in dynamic Guaymas Basin hydrothermal sediments.Nature communications · 2018Article
- Characterization of membrane-bound sulfane reductase: A missing link in the evolution of modern day respiratory complexes.The Journal of biological chemistry · 2018Article
- Structure of an Ancient Respiratory System.Cell · 2018Article
- Robust Production, Crystallization, Structure Determination, and Analysis of [Fe-S] Proteins: Uncovering Control of Electron Shuttling and Gating in the Respiratory Metabolism of Molybdopterin Guanine Dinucleotide Enzymes.Methods in enzymology · 2018Article
- Expanding the substrates for a bacterial hydrogenlyase reaction.Microbiology (Reading, England) · 2017Article
- The renaissance of life near the boiling point - at last, genetics and metabolic engineering.Microbial biotechnology · 2017Article
- HydDB: A web tool for hydrogenase classification and analysis.Scientific reports · 2016Article
- Characterization of the [3Fe-4S](0/1+) cluster from the D14C variant of Pyrococcus furiosus ferredoxin via combined NRVS and DFT analyses.Dalton transactions (Cambridge, England : 2003) · 2016Article
- Heterologous Production of an Energy-Conserving Carbon Monoxide Dehydrogenase Complex in the Hyperthermophile Pyrococcus furiosus.Frontiers in microbiology · 2016Article
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10 authors.
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Abstract
The archaeon Pyrococcus furiosus grows optimally at 100 °C by converting carbohydrates to acetate, CO2, and H2, obtaining energy from a respiratory membrane-bound hydrogenase (MBH). This conserves energy by coupling H2 production to oxidation of reduced ferredoxin with generation of a sodium ion gradient. MBH is encoded by a 14-gene operon with both hydrogenase and Na(+)/H(+) antiporter modules. Herein a His-tagged MBH was expressed in P. furiosus and the detergent-solubilized complex purified under anaerobic conditions by affinity chromatography. Purified MBH contains all 14 subunits by electrophoretic analysis (13 subunits were also identified by mass spectrometry) and had a measured iron:nickel ratio of 15:1, resembling the predicted value of 13:1. The as-purified enzyme exhibited a rhombic EPR signal characteristic of the ready nickel-boron state. The purified and membrane-bound forms of MBH both preferentially evolved H2 with the physiological donor (reduced ferredoxin) as well as with standard dyes. The O2 sensitivities of the two forms were similar (half-lives of ∼ 15 h in air), but the purified enzyme was more thermolabile (half-lives at 90 °C of 1 and 25 h, respectively). Structural analysis of purified MBH by small angle x-ray scattering indicated a Z-shaped structure with a mass of 310 kDa, resembling the predicted value (298 kDa). The angle x-ray scattering analyses reinforce and extend the conserved sequence relationships of group 4 enzymes and complex I (NADH quinone oxidoreductase). This is the first report on the properties of a solubilized form of an intact respiratory MBH complex that is proposed to evolve H2 and pump Na(+) ions.
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