Inactivation of beef heart mitochondrial F1‐ATPase by the 2′,3′‐dialdehyde derivatives of adenine nucleotides

Abstract
Beef heart mitochondrial F1-ATPase was inactivated by the 2′,3′-dialdehyde derivatives of ATP, ADP and AMP (oATP, oADP, oAMP). In the absence of Mg2+, inactivation resulted from the binding of 1 mol nucleotide analog per active unit of F1. The most efficient analog was oADP, followed by oAMP and oATP. Complete inactivation was correlated with the binding of about 11 mol [14C]oADP/mol F1. After correction for non-specific labeling, the number of specifically bound [14C]oADP was 2–3 mol per mol F1. By SDS-polyacrylamide gel electrophoresis, [14C]oADP was found to bind covalently mainly to the α and β subunits. In the presence of Mg2+, oATP behaved as a substrate and was slowly hydrolyzed.

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