Abstract
The transient kinetics of bovine heart mitochondrial ATPase (F 1) depleted of loosely bound nucleotides were observed. The activation process which was shown as a lag time before steady-state hydrolysis observed previously (Clark et al. (1984) Arch. Biochem. Biophys. 233, 378–392) was preceded by a proton burst when F 1 was stripped of its loose nucleotides. 5′-Adenylylimidodiphosphate (Ado PP[NH] P or MgATP binding is shown to cause proton release. Maximum proton release per F 1 free of loosely bound nucleotides is observed with MgATP. Modification with NBD-CL of F 1 that was nucleotide-depleted eliminated the proton burst, which suggests that the modified tyrosine (i.e., in the catalytic subunit) is directly involved in the release of protons.
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