Conformational transmission in ATP synthase during catalysis: Search for large structural changes
- 1 October 1996
- journal article
- Published by Springer Nature in Journal of Bioenergetics and Biomembranes
- Vol. 28 (5) , 409-414
- https://doi.org/10.1007/bf02113982
Abstract
Escherichia coli ATP synthase has eight subunits and functions through transmission of conformational changes between subunits. Defective mutation at βGly-149 was suppressed by the second mutations at the outer surface of the β subunit, indicating that the defect by the first mutation was suppressed by the second mutation through long range conformation transmission. Extensive mutant/pseudorevertant studies revealed that β/α and β/γ subunits interactions are important for the energy coupling between catalysis and H+ translocation. In addition, long range interaction between amino and carboxyl terminal regions of the γ subunit has a critical role(s) for energy coupling. These results suggest that the dynamic conformation change and its transmission are essential for ATP synthase.Keywords
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