Molecular biological studies on structure and mechanism of proton translocating ATPase (H+-ATPase, F0F1).
Recent results on ATPase, mainly from E. coli, obtained by biochemical and molecular biological approaches are reviewed, with special emphasis on results obtained in this laboratory. The advantages of using E. coli in studies of this important enzyme in oxidative phosphorylation are indicated: variant enzymes with specific amino acid replacements can be obtained and their functions and structures can be compared with those of the wild-type enzyme. Structural aspects of this complex enzyme are discussed, including the primary amino acid sequences and molecular assembly of subunits, and mechanistic aspects of the catalytic mechanism and proton translocation.
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005798:Genes, Bacterial; D009876:Operon; D006180:Proton-Translocating ATPases / Q000235:genetics* / Q000378:metabolism
D006180:Proton-Translocating ATPases