title: A proposal for the site and mechanism of redox-linked proton translocation in cytochrome c oxidase.
abstract: In this paper, we present a detailed mechanistic model for the redox-linked proton pump of cytochrome c oxidase. Using the spectroscopic properties of CuA, we have constructed a molecular orbital model for the electronic structure of the CuA site. One prediction of this model is that a ligand rearrangement should occur upon reduction of CuA. We further describe a detailed mechanism for proton pumping which utilizes this redox-linked CuA ligand rearrangement as its central feature. The turnover cycle of this proton pump model is then discussed in terms of the theoretical thermodynamic and kinetic requirements of a redox-linked proton pump.
authors.affiliation: Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
authors.forename: S I
authors.initials: SI
authors.lastname: Chan
authors.forename: P M
authors.initials: PM
authors.lastname: Li
authors.forename: T
authors.initials: T
authors.lastname: Nilsson
authors.forename: J
authors.initials: J
authors.lastname: Gelles
authors.forename: D F
authors.initials: DF
authors.lastname: Blair
authors.forename: C T
authors.initials: CT
authors.lastname: Martin
mesh_terms: D001665:Binding Sites; D003300:Copper / Q000378:metabolism; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011522:Protons; D013816:Thermodynamics
chemical_list: D008024:Ligands; D011522:Protons; D003300:Copper; D003576:Electron Transport Complex IV