publication . Other literature type . Article . 2018

Network analysis of a proposed exit pathway for protons to the P-side of cytochrome c oxidase

Cai, Xiuhong; Haider, Kamran; Lu, Jianxun; Radic, Slaven; Son, Chang Yun; Cui, Qiang; Gunner, M. R.;
  • Published: 01 Oct 2018
  • Publisher: Elsevier BV
  • Country: United States
Abstract
Abstract Cytochrome c Oxidase (CcO) reduces O2, the terminal electron acceptor, to water in the aerobic, respiratory electron transport chain. The energy released by O2 reductions is stored by removing eight protons from the high pH, N-side, of the membrane with four used for chemistry in the active site and four pumped to the low pH, P-side. The proton transfers must occur along controllable proton pathways that prevent energy dissipating movement towards the N-side. The CcO N-side has well established D- and K-channels to deliver protons to the protein interior. The P-side has a buried core of hydrogen-bonded protonatable residues designated the Proton Loading...
Subjects
free text keywords: Biophysics, Cell Biology, Biochemistry, Crystallography, Respiratory electron transport chain, Electron acceptor, chemistry.chemical_classification, chemistry, Protonation, Proton, Membrane, Biology, Hydrogen bond, Active site, biology.protein, Electrochemical gradient
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publication . Other literature type . Article . 2018

Network analysis of a proposed exit pathway for protons to the P-side of cytochrome c oxidase

Cai, Xiuhong; Haider, Kamran; Lu, Jianxun; Radic, Slaven; Son, Chang Yun; Cui, Qiang; Gunner, M. R.;