Abstract
Kinetics of the reduction of the hemes in cytochrome c oxidase in the presence of high concentration of ruthenium(III)hexaammine chloride was examined using a stopped-flow spectrophotometer. Upon mixing of the oxidized enzyme with dithionite and Ru(NH3) 3+6 , three well-resolved phases were observed: heme a reduction reaching completion within a few milliseconds is followed by two slow phases of heme a 3 reduction. The difference spectrum of heme a 3 reduction in the visible region is characterized by a maximum at ∼612 nm, rather than at 603 nm as was believed earlier. It is shown that in the case of bovine heart cytochrome c oxidase containing a special cation-binding site in which reversible binding of calcium ion occurs, heme a 3 reduction is slowed down by low concentrations of Ca2+. The effect is absent in the case of the bacterial cytochrome oxidase in which the cation-binding site contains a tightly bound Ca2+ ion. The data corroborate the inhibition of the cytochrome oxidase enzymatic activity by Ca2+ ions discovered earlier and indicate that the cation affects intramolecular electron transfer.
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Abbreviations
- CBS:
-
cation-binding site
- COX:
-
cytochrome c oxidase
- RuAm:
-
hexaammineruthenium (Ru(NH3) 3+6 )
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Published in Russian in Biokhimiya, 2012, Vol. 77, No. 8, pp. 1095–1104.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM12-049, June 17, 2012.
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Vygodina, T.V., Dyuba, A.V. & Konstantinov, A.A. Effect of calcium ions on electron transfer between hemes a and a 3 in cytochrome c oxidase. Biochemistry Moscow 77, 901–909 (2012). https://doi.org/10.1134/S0006297912080111
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DOI: https://doi.org/10.1134/S0006297912080111