Models of the two heme centers in cytochrome oxidase. The optical properties of cytochrome a and a3.
High and low spin complexes of ferric and ferrous heme a have been prepared and characterized spectroscopically. Bis(1-methylimidazole) heme a provides a good model for cytochrome a in both oxidation states while several spectral properties of cytochrome a3 can be reproduced by 1,2-dimethylimidazole heme a3. The visible absorbance spectra of these analogs account well for the absorbance spectra of oxidized and reduced cytochrome oxidase and support the conclusion (Vanneste, W. (1966) Biochemistry 5, 838-848) that cytochrome a provides the major contribution to the spectral changes in the 600 nm band upon reduction. The 655 nm band present in cytochrome oxidase appears to be a characteristic of high spin heme a+3.
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D017936:Cytochrome a Group; D003580:Cytochromes / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000378:metabolism*; D006418:Heme / Q000032:analysis*; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
D017936:Cytochrome a Group; D003580:Cytochromes; D006418:Heme; D003576:Electron Transport Complex IV