IR signatures of the metal centres of bovine cytochrome c oxidase: assignments and redox-linkage.
Assignments of IR bands of reduced minus oxidized IR difference spectra of bovine and related cytochrome c oxidases are reviewed and their linkages to specific metal centres are assessed. To aid this, redox-poised difference spectra in the presence of cyanide or carbon monoxide are presented. These ligands fix the redox states of either haem a3 alone or haem a3 and CuB respectively, while allowing redox cycling of the remaining centres.
*Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, U.K.
Raksha
R
Dodia
Amandine
A
Maréchal
Simona
S
Bettini
Masayo
M
Iwaki
Peter R
PR
Rich
D000818:Animals; D002248:Carbon Monoxide / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D003300:Copper / Q000737:chemistry; D003486:Cyanides / Q000737:chemistry; D003576:Electron Transport Complex IV / Q000737:chemistry*; D006418:Heme / Q000031:analogs & derivatives* / Q000737:chemistry; D007259:Infrared Rays; D008024:Ligands; D010084:Oxidation-Reduction / Q000528:radiation effects; D017550:Spectroscopy, Fourier Transform Infrared
D003486:Cyanides; D008024:Ligands; C027728:heme a; D006418:Heme; D003300:Copper; D002248:Carbon Monoxide; D003576:Electron Transport Complex IV