Browsing by Subject "Fumarate reduction"

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    Functionality of the Na+-translocating NADH:quinone oxidoreductase and quinol:fumarate reductase from Prevotella bryantii inferred from homology modeling
    (2024) Hau, Jann-Louis; Schleicher, Lena; Herdan, Sebastian; Simon, Jörg; Seifert, Jana; Fritz, Günter; Steuber, Julia; Hau, Jann-Louis; Institute of Biology, University of Hohenheim, Garbenstraße 30, 70599, Stuttgart, Germany; Schleicher, Lena; Institute of Biology, University of Hohenheim, Garbenstraße 30, 70599, Stuttgart, Germany; Herdan, Sebastian; Institute of Biology, University of Hohenheim, Garbenstraße 30, 70599, Stuttgart, Germany; Simon, Jörg; Microbial Energy Conservation and Biotechnology, Department of Biology, Technical University of Darmstadt, Schnittspahnstraße 10, 64287, Darmstadt, Germany; Seifert, Jana; HoLMiR-Hohenheim Center for Livestock Microbiome Research, University of Hohenheim, Leonore-Blosser-Reisen-Weg 3, 70599, Stuttgart, Germany; Fritz, Günter; Institute of Biology, University of Hohenheim, Garbenstraße 30, 70599, Stuttgart, Germany; Steuber, Julia; Institute of Biology, University of Hohenheim, Garbenstraße 30, 70599, Stuttgart, Germany
    Members of the family Prevotellaceae are Gram-negative, obligate anaerobic bacteria found in animal and human microbiota. In Prevotella bryantii , the Na + -translocating NADH:quinone oxidoreductase (NQR) and quinol:fumarate reductase (QFR) interact using menaquinone as electron carrier, catalyzing NADH:fumarate oxidoreduction. P. bryantii NQR establishes a sodium-motive force, whereas P. bryantii QFR does not contribute to membrane energization. To elucidate the possible mode of function, we present 3D structural models of NQR and QFR from P. bryantii to predict cofactor-binding sites, electron transfer routes and interaction with substrates. Molecular docking reveals the proposed mode of menaquinone binding to the quinone site of subunit NqrB of P. bryantii NQR. A comparison of the 3D model of P. bryantii QFR with experimentally determined structures suggests alternative pathways for transmembrane proton transport in this type of QFR . Our findings are relevant for NADH-dependent succinate formation in anaerobic bacteria which operate both NQR and QFR.