Sebastian Herdan (Stuttgart / DE), Jann-Louis Hau (Stuttgart / DE), Lena Schleicher (Stuttgart / DE), Jörg Simon (Darmstadt / DE), Jana Seifert (Stuttgart / DE), Günter Fritz (Stuttgart / DE), Julia Fritz-Steuber (Stuttgart / DE)
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.