Proton Transfer through a Charged Conduit in Respiratory Complex I: Long-Range Effects and Conformational Gating.

ABSTRACT: Energy coupling processes in respiratory complex I, a large redox-driven proton pump in the inner mitochondrial membrane, remain one of the most enigmatic problems in modern bioenergetics. Recent high-resolution cryo-EM structures of complex I revealed extensive hydration in the interior of the protein, including the buried E channel, which is an acidic charged conduit that bridges the quinone binding cavity with the extended membrane domain of the enzyme. Despite the general agreement that E channel participates in proton transfer, the absence of proton density in the cryo-EM maps poses a significant challenge to develop viable models of proton pumping. By adhering to the hypothesis that E channel catalyzes transfer of proton(s) from the quinone binding cavity to the membrane-bound proton

SUBMITTER: Simsive L 

PROVIDER: S-EPMC12529768 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature