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Showing 1 to 3 of 3 for “"Pi binding"”.
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Molecular Modulation of a-Subunit VISIT-DG Sequence Residue Asp-350 in the Catalytic sites of <em>Escherichia coli</em> ATP Synthase.
… critical amino acid residues involved in Pi binding have to be identified. The αVISIT-DG sequence at the interface of α/β subunits that contains residues from 345-351 is highly conserved and αAsp-350 has been chosen because of its negative charge side chain and its close proximity (~2.8 Å) …
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Role of a-Subunit VISIT-DG Sequence Residues Ile-346 and Ile-348 in the Catalytic Sites of Escherichia Coli ATP Synthase.
… α-subunit VISIT-DG sequence that is close to the Pi binding subdomain. The questions arise "Are they involved in Pi binding? Or are they there simply for the structural integrity of the catalytic sites?" Here, αIle-346and αIle-348, two important residues of the conserved VISIT-DG sequence, are …
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Intrinsic uncoupling in the ATP synthase of Escherichia coli. Studies on WT and ε-truncated mutants
… when the concentration of either ADP or Pi is maintained at a low level (Turina et al., 2004). The present work has dealt with the ATP synthase of E.coli, looking for evidence of this phenomenon of intrinsic uncoupling in this organism as well. First of all, we have shown that the …