Abstract
Abstract 1. Submitochondrial particles from beef heart, that were partially depleted of coupling factors, required the addition of coupling Factors 1 and 4 to catalyze the adenosine triphosphate-dependent H218O-inorganic phosphate exchange and the H218O-ATP exchange. The H218O-Pi exchange during succinate oxidation required catalytic amounts of adenine nucleotide as well as both coupling factors. An antiserum against coupling Factor 1 inhibited this exchange. 2. Levels of oligomycin which stimulated oxidative phosphorylation markedly inhibited the H218O-Pi exchange that took place under the same conditions. Both the H218O-Pi and the H218O-ATP exchange reactions were inhibited when ADP was removed by an ATP-regenerating system. The H218O-ATP exchange was stimulated by Pi. The significance of these findings with respect to current concepts of the mechanism of oxidative phosphorylation is discussed.
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