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J. Biol. Chem., Vol. 277, Issue 15, 13281-13285, April 12, 2002

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F₀ of ATP Synthase Is a Rotary Proton Channel
OBLIGATORY COUPLING OF PROTON TRANSLOCATION WITH ROTATION OF c-SUBUNIT RING^*

Toshiharu Suzuki^§, Hiroshi Ueno, Noriyo Mitome, Junko Suzuki, and Masasuke Yoshida^§¶

From the  Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama, 226-8503 and the ^§ ATP System Project, ERATO, Japan Science and Technology Corporation (JST), Nagatsuta 5800-3, Yokohama, 226-0026, Japan

Coupling of proton flow and rotation in the F₀ motor of ATP synthase was investigated using the thermophilic Bacillus PS3 enzyme expressed functionally in Escherichia coli cells. Cysteine residues introduced into the N-terminal regions of subunits b and c of ATP synthase (bL2C/cS2C) were readily oxidized by treating the expressing cells with CuCl₂ to form predominantly a b-c cross-link with b-b and c-c cross-links being minor products. The oxidized ATP synthases, either in the inverted membrane vesicles or in the reconstituted proteoliposomes, showed drastically decreased proton pumping and ATPase activities compared with the reduced ones. Also, the oxidized F₀, either in the F₁-stripped inverted vesicles or in the reconstituted F₀-proteoliposomes, hardly mediated passive proton translocation through F₀. Careful analysis using single mutants (bL2C or cS2C) as controls indicated that the b-c cross-link was responsible for these defects. Thus, rotation of the c-oligomer ring relative to subunit b is obligatory for proton translocation; if there is no rotation of the c-ring there is no proton flow through F₀.

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