Insights into functions of the H channel of cytochrome <i>c</i> oxidase from atomistic molecular dynamics simulations.

ABSTRACT: Proton pumping A-type cytochrome c oxidase (CcO) terminates the respiratory chains of mitochondria and many bacteria. Three possible proton transfer pathways (D, K, and H channels) have been identified based on structural, functional, and mutational data. Whereas the D channel provides the route for all pumped protons in bacterial A-type CcOs, studies of bovine mitochondrial CcO have led to suggestions that its H channel instead provides this route. Here, we have studied H-channel function by performing atomistic molecular dynamics simulations on the entire, as well as core, structure of bovine CcO in a lipid-solvent environment. The majority of residues in the H channel do not undergo large conformational fluctuations. Its upper and middle regions have a

SUBMITTER: Sharma V 

PROVIDER: S-EPMC5715751 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature