Baker, Gary M.
M.S. (Master of Science)
Department of Chemistry
The effect of temperature on the two heme centers has been examined in cytochrome c oxidase that was solubilized in n-dodecyl (3-D-maltoside (DM). The goal of the work was to systematically find experimental conditions that resolved selective thermal effects on the two hemes. We focused on spectral changes occuring at 45°C in high DM concentration. Under these conditions, we observed isosbestic points and a new charge transfer band at 635 nm. Reduced minus oxidized spectra of cytochromes a and a3 were resolved to identify thermally induced changes in each heme. The 635 nm band was assigned to cytochrome a. Loss of the 655 nm band, due to high spin cytochrome a3 was also observed, indicating that both hemes were thermally sensitive. A binding study of formate and cyanide was also used to selectively probe cytochromes a and a3
Yergul, E. Serap, "Use of temperature to selectively probe the cytochrome a and a? centers of bovine heart cytochrome c oxidase" (1994). Graduate Research Theses & Dissertations. 6582.
Northern Illinois University
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