Abstract
The molecular mechanism of ATP synthesis and hydrolysis carried out by the F0.F1 enzyme complex is still unknown. A large number of studies using different approaches point to the F1-β subunit as the one that contains the catalytic site and is involved, “together with the α subunit, in substrate binding (1–4). A detailed characterization of substrate binding sites on F1 and their relation to its catalytic site is, however, very difficult because of the complexity of the F1 structure. A promising approach to the elucidation of this problem is the study of isolated, functionally active, α and β subunits.
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Gromet-Elhanan, Z. (1987). Characterization of the Catalytic Site on the β Subunit of the H+-ATP Synthase-ATPase Complex and Demonstration of Functional Homology of β Subunits Isolated from Different Sources. In: Biggins, J. (eds) Progress in Photosynthesis Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0516-5_15
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DOI: https://doi.org/10.1007/978-94-017-0516-5_15
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