Carboxyl group functions in the heme-copper oxidases: information from mid-IR vibrational spectroscopy.
Carboxyl groups of possible functional importance in bovine and bacterial cytochrome c oxidases (CcO) are reviewed and assessed. A critical analysis is presented of available mid-infrared vibrational data that pertain to these functional carboxyl groups. These data and their interpretations are discussed in relation to current models of the mechanism of proton and electron coupling in the protonmotive CcO superfamily.
Rich
Peter R
PR
Glynn Laboratory of Bioenergetics, Department of Biology, University College London, Gower Street, London WC1E 6BT, UK. PRR@UCL.AC.UK
Maréchal
Amandine
A
D000818:Animals; D001224:Aspartic Acid; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D002264:Carboxylic Acids / Q000378:metabolism; D002417:Cattle; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D019216:Metals, Heavy / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D012964:Sodium / Q000378:metabolism; D013055:Spectrophotometry, Infrared; D017550:Spectroscopy, Fourier Transform Infrared; D014732:Vibration
D002264:Carboxylic Acids; D019216:Metals, Heavy; D021122:Protein Subunits; D001224:Aspartic Acid; D012964:Sodium; D003576:Electron Transport Complex IV; D002118:Calcium