Abstract
The F1FO proton translocating ATP synthetases1 from mitochondrial, chloroplast thylakoids and bacterial plasma membranes are the principal catalyst in the transduction of energy derived from electron transport (1–3). These enzyme complexes are generally composed of an integral membrane sector, FO, which mediates H+ translocation, and a peripheral protein sector, F1 which catalyzes the terminal step of ATP synthesis from ADP and Pi. F1 is composed of five different polypeptide chains designated α-ε in order of decreasing Mr. The molecular weight of F1 is about 380, 000 and the subunit stoichiometry is α3β3γδε. The binding sites for ADP and ATP are located on the α and β subunits and the catalytic sites are thought to be on the β subunits. The F1-ATPases from mitochondria (MFj) and E. coli (EF1) were shown to contain six nucletide binding sites (1, 2). The F1-ATPase from the thermophilic bacterium, PS3 (TF1), contains at least four nucleotide binding sites (4) and CF1, from chloroplast thylakoid membranes, contains three nucleotide binding sites (5, 6). TF1 has three noncatalytic nucleotide binding sites putatively in the α subunits and at least one catalytic site on the β subunit (4). Soluble CF1 has two sites where ADP can bind, and in the presence of Mg2+ and ATP, another single site for ATP was described (6). Tight binding of ADP and ATP to the membrane bound CF1 was also described (7–10). Although the role of these nucleotide binding sites has been studied extensively, it is difficult to distinguish between nucleotides bound at catalytic and noncatalytic sites. Several lines of evidence amply documented by Boyer and coworkers (7) support the participation of tightly bound nucleotides as catalytic intermediated in ATP synthesis and hydrolysis.
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© 1987 Springer Science+Business Media Dordrecht
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Shavit, N. (1987). Localization of the nucleotide binding sites on subunits of CF1 and TF1 using the photoreactive nucleotide analog 3-O-(4-benzoyl) benzoyl ATP. In: Biggins, J. (eds) Progress in Photosynthesis Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0516-5_1
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DOI: https://doi.org/10.1007/978-94-017-0516-5_1
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