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Conformational transmission in ATP synthase during catalysis: Search for large structural changes

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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.

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Authors and Affiliations

  1. Division of Biological Sciences, The Institute of Scientific and Industrial Research, Osaka University, Ibaraki, 567, Osaka, Japan

    Masamitsu Futai & Hiroshi Omote

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  1. Masamitsu Futai
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  2. Hiroshi Omote
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Futai, M., Omote, H. Conformational transmission in ATP synthase during catalysis: Search for large structural changes. J Bioenerg Biomembr 28, 409–414 (1996). https://doi.org/10.1007/BF02113982

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  • DOI: https://doi.org/10.1007/BF02113982

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