title: Two ATPases.
abstract: In this article, I reflect on research on two ATPases. The first is F(1)F(0)-ATPase, also known as ATP synthase. It is the terminal enzyme in oxidative phosphorylation and famous as a nanomotor. Early work on mitochondrial enzyme involved purification in large amount, followed by deduction of subunit composition and stoichiometry and determination of molecular sizes of holoenzyme and individual subunits. Later work on Escherichia coli enzyme utilized mutagenesis and optical probes to reveal the molecular mechanism of ATP hydrolysis and detailed facets of catalysis. The second ATPase is P-glycoprotein, which confers multidrug resistance, notably to anticancer drugs, in mammalian cells. Purification of the protein in large quantity allowed detailed characterization of catalysis, formulation of an alternating sites mechanism, and recently, advances in structural characterization.
authors: Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA. alan_senior@urmc.rochester.edu
authors: Alan E
authors: AE
authors: Senior
mesh_terms: D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1 / Q000235:genetics / Q000266:history / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000235:genetics / Q000378:metabolism; D000818:Animals; D018432:Drug Resistance, Multiple / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D006868:Hydrolysis; D016296:Mutagenesis; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000266:history / Q000378:metabolism*
chemical_list: D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1; D029968:Escherichia coli Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases