Structure and function of the ATPase-ATP synthase complex of mitochondria as compared to chloroplasts and bacteria.
An overview of the structure and function of the mitochondrial ATPase-ATP synthase complex is presented. Attempts are made to identify the analogies and differences between mitochondrial, chloroplastic and bacterial complexes. The relatively more precise information available on the structure of the E. coli enzyme is used to try and understand the apparently more complex structure of the mitochondrial enzyme. Recent ideas on the mechanism of ATP hydrolysis and ATP synthesis will be summarized.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology*; D055598:Chemical Phenomena; D002621:Chemistry; D002736:Chloroplasts / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology; D006868:Hydrolysis; D008928:Mitochondria / Q000201:enzymology*; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D011522:Protons
D011522:Protons; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases