Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.

@article{Liang2017UnderstandingTE,
  title={Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.},
  author={Ruibin Liang and Jessica M. J. Swanson and M{\aa}rten Wikstr{\"o}m and Gregory A. Voth},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2017},
  volume={114 23},
  pages={
          5924-5929
        }
}
Cytochrome c oxidase (CcO) catalyzes the reduction of oxygen to water and uses the released free energy to pump protons against the transmembrane proton gradient. To better understand the proton-pumping mechanism of the wild-type (WT) CcO, much attention has been given to the mutation of amino acid residues along the proton translocating D-channel that impair, and sometimes decouple, proton pumping from the chemical catalysis. Although their influence has been clearly demonstrated… CONTINUE READING

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