The H channel is not a proton transfer path in yeast cytochrome c oxidase

Biochimica Et Biophysica Acta. Bioenergetics
Aapo MalkamäkiVivek Sharma

Abstract

Cytochrome c oxidases (CcOs) in the respiratory chains of mitochondria and bacteria are primary consumers of molecular oxygen, converting it to water with the concomitant pumping of protons across the membrane to establish a proton electrochemical gradient. Despite a relatively well understood proton pumping mechanism of bacterial CcOs, the role of the H channel in mitochondrial forms of CcO remains debated. Here, we used site-directed mutagenesis to modify a central residue of the lower span of the H channel, Q413, in the genetically tractable yeast Saccharomyces cerevisiae. Exchange of Q413 to several different amino acids showed no effect on rates and efficiencies of respiratory cell growth, and redox potential measurements indicated minimal electrostatic interaction between the 413 locus and the nearest redox active component heme a. These findings clearly exclude a primary role of this section of the H channel in proton pumping in yeast CcO. In agreement with the experimental data, atomistic molecular dynamics simulations and continuum electrostatic calculations on wildtype and mutant yeast CcOs highlight potential bottlenecks in proton transfer through this route. Our data highlight the preference for neutral residues in ...Continue Reading

Citations

Jul 14, 2020·Biotechnology and Applied Biochemistry·Linda LeoneAngela Lombardi
Mar 11, 2020·Proceedings of the National Academy of Sciences of the United States of America·Hanna KwonEmma L Raven
Apr 16, 2020·Proceedings of the National Academy of Sciences of the United States of America·Amandine MaréchalPeter R Rich
Aug 24, 2021·Frontiers in Molecular Biosciences·Marco ReidelbachVivek Sharma

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