Abstract
The effect of ATP and other anions on the kinetics of cytochromec oxidation by reconstituted bovine heart cytochromec oxidase was investigated. The following results were obtained: (1) ATP and other polyvalent anions increase theK m for cytochromec and theV max (if assayed by the photometric method). The magnitude of the effect is proportional to the charge of the anion as follows from the series of increasing effectiveness: Pi<AMP<ADP<PPi<ATP<PPPi. (2) The kinetic effects are obtained in the millimolar physiological concentration range. (3) The kinetic changes are not saturated at high concentrations. (4) A specific interaction site for ATP at the cytosolic domain of the enzyme is concluded from the increase ofK m for cytochromec after photolabelling of proteoliposomes with 8-azido-[γ-32P]-ATP, which is protected by ATP but not by ADP. (5) No specific “binding site” for ATP could be identified by photolabelling with 8-azido-[γ-32P]-ATP. The labelling is only partly protected by ATP or ADP.
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Abbreviations
- CCP:
-
carbonylcyanide-m-chlorophenylhydrazone
- TMPD:
-
N,N,N′,N′-tetramethyl-1,4-phenylenediamine dihydrochloride
- 8-N3-ATP:
-
8-azido-adenosine-5′-triphosphate
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Dedicated to Professor Dr. Friedhelm Schneider on the occasion of his 60th birthday.
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Hüther, FJ., Berden, J. & Kadenbach, B. Influence of 8-azido-ATP and other anions on the activity of cytochromec oxidase. J Bioenerg Biomembr 20, 503–516 (1988). https://doi.org/10.1007/BF00762206
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DOI: https://doi.org/10.1007/BF00762206