title: Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3.
abstract: The F-type ATPase, TF0F1, from the thermophilic Bacillus PS3, which is free of nucleotides after isolation, was specifically loaded with one 2-azido ADP on a non-catalytic site. The enzyme was covalently modified to various extents and the rate of ATP synthesis and ATP hydrolysis was measured. Both ATP synthesis and ATP hydrolysis extrapolated to zero for covalently binding one nucleotide per enzyme. This was interpreted such that the non-catalytic sites are involved in the coupled catalytic process.
authors.affiliation: Département de Biologie Cellulaire et Moléculaire, CEA Saclay, Gif-sur-Yvette, France.
authors.forename: P
authors.initials: P
authors.lastname: Richard
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism; D000345:Affinity Labels; D000595:Amino Acid Sequence; D001386:Azides; D001407:Bacillus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000378:metabolism; D001436:Bacteriorhodopsins / Q000378:metabolism; D001665:Binding Sites; D001693:Biological Transport, Active; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007700:Kinetics; D008081:Liposomes; D008567:Membranes, Artificial; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000378:metabolism
chemical_list: D000345:Affinity Labels; D001386:Azides; D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D008081:Liposomes; D008567:Membranes, Artificial; D001436:Bacteriorhodopsins; D000244:Adenosine Diphosphate; D006180:Proton-Translocating ATPases