The ATP‐ and ADP‐binding sites in mitochondrial coupling factor F₁ and their possible role in oxidative phosphorylation

The Structure of Proteins Involved in Active Membrane Transport

“…A variety of "tight" and "loose" nucleotide binding sites exist on all types of F I studied so far (8,19,154,195). Their role in ATPase activity is uncertain, however.…”

Changes in mitochondrial components of hamster brown adipose tissue in response to cold acclimation

“…Therefore, cytochrome c content seems to be a reasonable indicator of the respiratory capacity of brown adipose tissue. F1 ATPase activity should reflect phosphorylating capacity, since catalysis of ADP phosphorylation and of ATP hydrolysis is thought to occur at the same binding sites (Slater et aL, 1979). The low F1 ATPase activity in brown adipose tissue seen in this study correlates well with electron-microscopic studies (Lindberg et al, 1967) showing brown adipose tissue mitochondria inner membrane vesicles depleted in F1 ATPase.…”

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

“…These proteins are probably assembled with a stoichiometry of 3ca:3(3: Iy: 1l: le (Catterall and Pedersen, 1971;Bragg and Hou, 1975;Fillingame, 1981). An adenine nucleotide binding site appears to be present in each of the 3ca-and 3(3-subunits, making six in all (Slater et al, 1979;Wagenvoord et al, 1980). Covalent modification experiments indicate that ( contributes to catalysis (Ferguson et al, 1975;Esch and Allison, 1978;Drutsa et at., 1979;Yoshida et al, 1981a, 198 lb); also it is able to bind both ADP and ATP as required for catalysis (Harris, 1978;Wagenvoord et al, 1980).…”