S11.11 FTIR detection of carboxyl groups in bovine heart cytochrome c oxidase
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چکیده
منابع مشابه
COMMEMORATIVE LECTURE Reaction Mechanism of Bovine Heart Cytochrome Oxidase
As I mentioned at the awards ceremony a little while ago, the work for which I have received the Keio Med ical Award is not something that I have been able to accomplish alone; it has involved the cooperation of many scientists. Dr. Tsukihara is Professor of the Insti tute for Protein Research, Osaka University, and spe cializes in X-ray crystallography. Dr. Kitagawa and Dr. Ogura, who is here ...
متن کاملRedox-Controlled Proton Gating in Bovine Cytochrome c Oxidase
Cytochrome c oxidase is the terminal enzyme in the electron transfer chain of essentially all organisms that utilize oxygen to generate energy. It reduces oxygen to water and harnesses the energy to pump protons across the mitochondrial membrane in eukaryotes and the plasma membrane in prokaryotes. The mechanism by which proton pumping is coupled to the oxygen reduction reaction remains unresol...
متن کاملRedox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a signif...
متن کاملStructures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase.
All 13 lipids, including two cardiolipins, one phosphatidylcholine, three phosphatidylethanolamines, four phosphatidylglycerols and three triglycerides, were identified in a crystalline bovine heart cytochrome c oxidase (CcO) preparation. The chain lengths and unsaturated bond positions of the fatty acid moieties determined by mass spectrometry suggest that each lipid head group identifies its ...
متن کاملQuantitative reevaluation of the redox active sites of crystalline bovine heart cytochrome c oxidase.
Approximately 30% of the iron contained in a bovine heart cytochrome c oxidase preparation was removed by crystallization, giving a molecular extinction coefficient 1.25-1.4 times higher than those reported thus far. Six electron equivalents provided by dithionite were required for complete reduction of the crystalline cytochrome c oxidase preparation. The fully reduced enzyme was oxidized with...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Bioenergetics
سال: 2008
ISSN: 0005-2728
DOI: 10.1016/j.bbabio.2008.05.266