Properties and regulation of the H+-ATP synthase of mitochondria.
A brief survey is made of the function of the H+-ATP synthase of mitochondria with emphasis on how it is regulated. A main regulatory factor is a low molecular weight protein whose binding to the enzyme appears to be essential for optimal accumulation of ATP as driven by electron transport. The ATP synthase is also controlled by ADP that, by binding to a site in the enzyme, inhibits ATP hydrolysis. Data on the spontaneous synthesis of a tightly bound ATP are discussed. Apparently, this requires proper subunit interactions to yield a competent catalytic site.
D000244:Adenosine Diphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D004563:Electrochemistry; D004579:Electron Transport; D008928:Mitochondria / Q000201:enzymology*; D008929:Mitochondria, Heart / Q000201:enzymology; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D012246:Rhodospirillum / Q000201:enzymology
D000244:Adenosine Diphosphate; D006180:Proton-Translocating ATPases