A cytochrome c oxidase proton pumping mechanism that excludes the O2 reduction site.
A redox-coupled conformational change in Asp51 of subunit I and a hydrogen-bond network connecting Asp51 with the matrix surface have been deduced from X-ray structures of bovine heart cytochrome c oxidase. This has provided evidence that Asp51 may play a role in the proton pumping process. However, the lack of complete conservation of a residue analogous to Asp51, the inclusion of a peptide bond in the hydrogen-bonding network and the lack of apparent involvement of the O2 reduction site have been used as arguments against the involvement of Asp51 in the mechanism of proton pumping. This minireview re-examines these arguments.
Yoshikawa
Shinya
S
Department of Life Science, Himeji Institute of Technology, Kamighori Ako, Hyogo 678-1297, Japan. yoshi@sci.himeji-tech.ac.jp
D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry; D002417:Cattle; D018360:Crystallography, X-Ray; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D066298:In Vitro Techniques; D008958:Models, Molecular; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017494:Proton Pumps / Q000737:chemistry / Q000378:metabolism; D018892:Proton-Motive Force
D017494:Proton Pumps; D001224:Aspartic Acid; D003576:Electron Transport Complex IV