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Free keywords:
Inhibition; ATP synthesis; Tritiated N-propylhydroxylamine; H+-jump;
Modified proteolipid; DCCD; dicyclohexylcarbodiimide; 3H-PHA;
[2,3-3H]propylhydroxylamine; SDS-PAGE; sodium dodecylsulfate polyacrylamide gel electrophoresis
Abstract:
ATP synthesis of TF1·Fo liposomes in proton‐jump experiments was inhibited by N‐[2,3‐3H]propylhydroxylamine. High radioactivity was shown by SDS‐PAGE to be incorporated into the proteolipid. The activation of one of its carboxyl groups, which was apparently trapped by the hydroxylamine derivative, may proceed by the protonation of an undissociated carboxyl group as part of the proton translocation. If ADP was omitted, no trapping reaction occurred. Thus binding of ADP to TF1 appeared to be necessary for such an activation of a carboxyl group.
