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pubmed:abstractText |
In common with the F1-ATPase from other sources, yeast mitochondrial F1-ATPase was inhibited by 4-chloro-7-nitrobenzofurazan. Total inhibition of the F1-ATPase activity was compatible with the modification of a single tyrosine residue per F1-ATPase molecule. Radioactive labelling experiments localized this modification on a beta-subunit. The inactive modified enzyme retained the capacity to bind the photoaffinity label 8-azido-1,N6-etheno-ATP, which has previously been shown to bind nucleotide sites of low affinity. As well, the inactive modified enzyme bound MgATP with high affinity, yielding a Kd of 14 microM. The results are consistent with the hypothesis of alternating, or cooperative, site catalysis by F1-ATPase.
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