Abstract
Cytochrome c oxidase from bovine heart contains seven binding sites for ATP or ADP and three additional for ADP only, as concluded from competition equilibrium dialysis binding studies. The isolated enzyme contains bound cholate which, in contrast to bound ATP, is only slowly exchanged by ADP (or ATP). The kinetics of the reconstituted enzyme is influenced by extraliposomal (cytosolic) ATP and ADP. The Km for cytochrome c is five times higher in the presence of extraliposomal ATP than of ADP. These differences of Km values are lost after preincubation of the enzyme with a monoclonal antibody to subunit IV. The data demonstrate regulation of cytochrome c oxidase activity by the cytosolic ATP/ADP-ratio, in addition to regulation by the matrix ATP/ADP-ratio [Arnold and Kadenbach (1997) Eur. J. Biochem. 249, 350- 354], both interacting with subunit IV.
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