The site of the redox-linked proton pump in eukaryotic cytochrome c oxidases.
The electronic spectra of fully oxidized derivatives of some cytochrome c oxidase preparations are distinctly pH dependent. In general, the observed spectral shifts are greater in the case of pulsed derivatives compared to resting preparations and also, greater for preparations of the enzyme from shark skeletal muscle compared to beef heart. The low temperature near-infrared magnetic circular dichroism spectrum of the fully oxidized shark enzyme is not pH dependent in the experimental range, indicating the sensitivity of the visible region electronic spectrum to variation in pH to be due principally to changes at the heme a3-CuB chromophore. The results are discussed in relation to proposed mechanisms of proton translocation in cytochrome c oxidase.
Holm
D E
DE
Department of Chemistry, University of Alabama, Tuscaloosa 35487-0336, USA.
Godette
G
G
Bonaventura
J
J
Bonaventura
C
C
Peterson
J
J
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008961:Models, Structural; D018482:Muscle, Skeletal / Q000201:enzymology; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017494:Proton Pumps / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012754:Sharks; D013053:Spectrophotometry
D017494:Proton Pumps; D003576:Electron Transport Complex IV