Abstract
The catalytic portion (F1) of ATP synthases have the subunit composition alpha 3, beta 3, gamma, delta, epsilon. This composition imparts structural asymmetry to the entire complex that results in differences in nucleotide binding affinity among the six binding sites. Evidence that two or more sites participate in catalysis, alternating their properties, led to the notion that the interactions of individual alpha beta pairs with the small subunit must change as binding sites properties alternate. A rotation of the gamma subunit within the alpha 3 beta 3 hexamer has been proposed as a means of alternating the properties of catalytic sites. Evidence argues that the rotation of the complete gamma subunit during ATP hydrolysis is not mandatory for activity. The gamma subunit of chloroplast F1 may be cleaved into three large fragments that remain bound to F1. This cleavage enhances ATPase activity without loss of evidence of site-site interactions. Complexes of alpha 3 beta 3 have been shown to have significant ATPase activity in the absence of gamma. Mg2+ATP affects the interaction of gamma with the different beta subunits, and induces other changes in F1, but whether these changes are induced by catalysis, or are fast enough to be...Continue Reading
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