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Interactions of Ca/sup 2 +/ and H/sup +/ with heme A in cytochrome oxidase

Journal Article · · J. Bioenerg. Biomembr.; (United States)
DOI:https://doi.org/10.1007/BF00744692· OSTI ID:5615284

Ca/sup 2 +/ ions shift the absorption spectrum of reduced cytochrome a in mitochondria by acting from the outside of the membrane. In isolated cytochrome oxidase the shift may be induced by either Ca/sup 2 +/ or H/sup +/, the apparent pK varying between 6.20 and 5.75 depending on the state of cytochrome a3. Studies of the Soret band show that Ca/sup 2 +/ also shifts the spectrum of ferrocytochrome a3 in isolated oxidase in contrast to the situation in mitochondria or isolated oxidase reconstituted into liposomes. Model studies with reduced bis-imidazole heme A reveals an analogous spectral shift induced by Ca/sup 2 +/. Esterification of the propionate carboxyls of heme A abolishes the spectral shift, suggesting that it is due to interaction of Ca/sup 2 +/ with these groups. When taken together with the data with intact mitochondria, this suggests that the propionate side chains of cytochrome a are accessible to Ca/sup 2 +/ and H/sup +/ from the outside of the mitochondrial membrane. In the soluble enzyme both hemes a and a3 are accessible. Thus heme a may be located near the outside of the inner membrane whereas heme a3 experiences a different environment in which no Ca/sup 2 +/ shift occurs.

OSTI ID:
5615284
Journal Information:
J. Bioenerg. Biomembr.; (United States), Journal Name: J. Bioenerg. Biomembr.; (United States) Vol. 12:3-4; ISSN JBBID
Country of Publication:
United States
Language:
English