Add time:08/19/2019         Source:sciencedirect.com

4-Azido-2-nitrophenyl [α-32P]pyrophosphate (azido-[α-32p]PPi) mimics ADP and PP1 by some of its binding properties when assayed in the absence of photoirradiation with mitochondrial Fl-ATPase. Upon photoirradiation, both α- and β-subunits of F1-ATPase were covalently labelled. Following chemical and enzymatic cleavages of each of the two photolabelled subunits, peptides containing the covalently bound radioactivity were separated by HPLC and identified by amino acid sequencing. Bound azido-[α-32P]PPi was found to be concentrated in two distant sequences of the α-subunit, namely Asp194-Thr221 and Lys386-Met437, and in a single sequence of the β-subunit G1u294-Met358 with most of the photoprobe bound to β-Tyr-311 and β-Tyr-345. These results are discussed in terms of a model in which the pyrophosphate binding sites of F1 are located in regions of the α- and β-subunits exposed at the interface between the two subunits and correspond to non-catalytic and catalytic adenine nucleotide binding sites, respectively.

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