Mechanistic Principles of Hydrogen Evolution in the Membrane-Bound Hydrogenase.

ABSTRACT: The membrane-bound hydrogenase (Mbh) from Pyrococcus furiosus is an archaeal member of the Complex I superfamily. It catalyzes the reduction of protons to H₂ gas powered by a [NiFe] active site and transduces the free energy into proton pumping and Na⁺/H⁺ exchange across the membrane. Despite recent structural advances, the mechanistic principles of H₂ catalysis and ion transport in Mbh remain elusive. Here, we probe how the redox chemistry drives the reduction of the proton to H₂ and how the catalysis couples to conformational dynamics in the membrane domain of Mbh. By combining large-scale quantum chemical density functional theory (DFT) and correlated ab initio wave function methods with atomistic molecular dynamics si

SUBMITTER: Sirohiwal A 

PROVIDER: S-EPMC11228991 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature