Analysis of the spectra and redox properties of pure cytochromes aa3

• Published in: Biophysical journal 1986-03, Vol.49 (3), p.717-729
• Main Authors: Hendler, R.W., Reddy, K.V., Shrager, R.I., Caughey, W.S.
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Cattle; Electron Transport Complex IV - metabolism; Fundamental and applied biological sciences. Psychology; Hemoproteins; Hydrogen-Ion Concentration; Kinetics; Metalloproteins; Mitochondria, Heart - metabolism; Oxidation-Reduction; Proteins; Spectrophotometry; Thermodynamics
• ISSN: 0006-3495; 1542-0086
• DOI: 10.1016/S0006-3495(86)83698-0

The findings in the current studies with pure cytochrome aa3 confirm the findings in an accompanying paper pertaining to cytochrome aa3 in mitochondria (Reddy et al., 1985). In both cases, three Nernstian titrations are seen with Em values near 200, 260, 340 mV with n values of 2, 2, and 1. Similarly, the alpha absorption features of the difference spectra in both cases were centered near 602, 605, and 607 mn. The component with Em approximately 200 mV was identified as heme a3 on the basis of experiments conducted in an atmosphere of carbon monoxide, and in both cases, the carbon monoxide-liganded species did not display an elevated Em. In the current studies, unique Soret absorbance features are added to the difference spectra for the three Nernstian transitions. Specifically, absorption peaks at 429, 446, and 448 nm go with the alpha peaks seen respectively at 602, 605, and 607 nm. Evidence was presented to support the hypothesis that the redox state of heme alpha may control the redox potential of heme a3.