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The (aF357C)3(bR372C)3c subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 altered ATPase activity after cross-linking a and b subunits at noncatalytic site interfaces


The (aF357C)3(bR372C)3c subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 altered ATPase activity after cross-linking a and b subunits at noncatalytic site interfaces



Biochemistry (American Chemical Society) 41(9): 26-34



In crystal structures of bovine MFl, the side chains of aF357 and bR372 are near the adenines of nucleotides bound to noncatalytic sites. To determine if during catalysis these side chains must pass through the different arrangements in which they are present in crystal structures, the catalytic properties of the (aF357C)3(bR372C)3c subcomplex of the TF1-ATPase were characterized before and after cross-linking the introduced cysteines with CuCl2. The unmodified mutant enzyme hydrolyzes MgATP at 50% the rate exhibited by wild type. Detailed comparison of the catalytic properties of the double mutant enzyme before and after cross-linking with those of the wild-type subcomplex revealed the following. Before cross-linking, the (aF357C)3(bR372C)3c subcomplex has less tendency than wild type to release inhibitory MgADP entrapped in a catalytic site during turnover when MgADP binds to noncatalytic sites. Following cross-linking, ATPase activity is reduced 5-fold, and inhibitory MgADP entrapped in a catalytic site during turnover does not release under conditions wherein binding of ATP to noncatalytic sites of the wild-type enzyme promotes release of MgADP from the affected catalytic site. When assayed in the presence of lauryldimethylamine oxide, which prevents turnover-dependent entrapment of inhibitory MgADP in a catalytic site, ATPase activity of the cross-linked form is 47% that of the unmodified mutant enzyme. These results suggest that, during catalysis, the side chains of aF357 and bR372 do not pass through the extremely different relative positions in which they exist at the three noncatalytic site interfaces in crystal structures. Reprinted by permission of the publisher.

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