A Biological Molecular Motor, Proton-Translocating ATP Synthase: Multidisciplinary Approach for a Unique Membrane Enzyme |
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| Authors: | Yoshihiro Sambongi Ikuo Ueda Yoh Wada Masamitsu Futai |
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| Institution: | (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;(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 |
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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   c
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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| Keywords: | Escherichia coli motor ATP synthase FoF1 catalytic residues ion pump ATPase mechanochemistry c-subunit ring energy conversion |
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