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A Biological Molecular Motor, Proton-Translocating ATP Synthase: Multidisciplinary Approach for a Unique Membrane Enzyme

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Abstract

Proton-translocating ATP synthase (FoF1) synthesizes ATP from ADP and phosphate, coupled with an electrochemical proton gradient across the biological membrane. It has been established that the rotation of a subunit assembly is an essential feature of the enzyme mechanism and that FoF1 can be regarded as a molecular motor. Thus, experimentally, in the reverse direction (ATP hydrolysis), the chemical reaction drives the rotation of a γεc 10-14 subunit assembly followed by proton translocation. We discuss our very recent results regarding subunit rotation in Escherichia coli FoF1 with a combined biophysical and mutational approach.

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Authors and Affiliations

  1. Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, CREST (Core Research for Evolutional Science and Technology) of Japan Science and Technology Corporation, Ibaraki, Osaka, 567-0047, Japan

    Yoshihiro Sambongi, Ikuo Ueda & Yoh Wada

  2. Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, CREST (Core Research for Evolutional Science and Technology) of Japan Science and Technology Corporation, Ibaraki, Osaka, 567-0047, Japan

    Masamitsu Futai

Authors
  1. Yoshihiro Sambongi
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  2. Ikuo Ueda
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  3. Yoh Wada
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  4. Masamitsu Futai
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Sambongi, Y., Ueda, I., Wada, Y. et al. A Biological Molecular Motor, Proton-Translocating ATP Synthase: Multidisciplinary Approach for a Unique Membrane Enzyme. J Bioenerg Biomembr 32, 441–448 (2000). https://doi.org/10.1023/A:1005656706248

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