Functional Dynamics of an Ancient Membrane-Bound Hydrogenase
Max E. Mühlbauer, Ana P. Gámiz‐Hernández, Ville R. I. Kaila
Abstract
binding and protonation changes at a putative ion-binding site couple to proton transfer across the antiporter-like MbhH subunit by modulating the conformational state of a conserved ion pair at the subunit interface. Our findings illustrate conserved coupling principles within the complex I superfamily and provide functional insight into archaeal energy transduction mechanisms.
Topics & Concepts
ChemistryHydrogenaseAntiporterPyrococcus furiosusArchaeaProtonationAntiportersMolecular dynamicsBiophysicsProtein subunitBioenergeticsMembraneIonBiochemistryComputational chemistryEnzymeBiologyGeneMitochondrionOrganic chemistryMetalloenzymes and iron-sulfur proteinsHydrogen Storage and MaterialsPhotosynthetic Processes and Mechanisms