RESUMO
Soluble F1 from beef heart that has been depleted of adenine nucleotides to values of 0.4 mol of ADP and 0.1 mol ATP/mol of enzyme has the capacity to synthetize about 0.1 mol of ATP/mol of enzyme from medium phosphate in the presence of Mg2+ and 30% dimethyl sulfoxide. Under the same conditions, native and adenine nucleotide depleted F1 can also synthesize pyrophosphate to values that range from 0.03 to 0.05 mol/mol of F1. The formation of pyrophosphate requires Mg2+ and dimethyl sulfoxide. The formed pyrophosphate remains bound to F1 during filtration through Sephadex centrifugation columns. In all water media, adenine nucleotide depleted, but not native, F1 can hydrolyze pyrophosphate to values of about 0.2 nmol min-1 mg-1. This activity is inhibited or stimulated by agents (adenylyl imidodiphosphate, aurovertin, and methanol) that produce such effects on the ATPase activity of F1; NaN3 stimulated the activity. Therefore, F1 from bovine heart mitochondria has the capacity to catalyze synthesis and hydrolysis of ATP. Synthesis of pyrophosphate by the soluble F1 appears to follow the same energetic considerations that have been postulated for ATP synthesis by the soluble enzyme [de Meis (1989) Biochim. Biophys. Acta 973, 339-349].
