Mutational analysis of F1F0 ATPase: catalysis and energy coupling.
Escherichia coli ATP synthase has eight subunits and functions through transmission of conformational changes between subunits. Extensive mutational analyses identified essential residues for catalysis and conformation transmission. Pseudorevertant studies revealed that beta/alpha and beta/gamma subunits interactions are important for the energy coupling between catalysis and H+ translocation. In this article, we discuss mechanism of catalysis and energy coupling based on our recent mutation studies.
Omote
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Division of Biological Sciences, Osaka University, Ibaraki, Japan.
Futai
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D000595:Amino Acid Sequence / Q000235:genetics; D002384:Catalysis; D004252:DNA Mutational Analysis; D004734:Energy Metabolism / Q000502:physiology; D004926:Escherichia coli / Q000201:enzymology; D025261:Mitochondrial Proton-Translocating ATPases; D008958:Models, Molecular; D009154:Mutation / Q000502:physiology; D006180:Proton-Translocating ATPases / Q000235:genetics* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D029701:Saccharomyces cerevisiae Proteins; C108166:ATP17 protein, S cerevisiae; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases