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Papers In Press, published online ahead of print January 28, 2002
Chemical resources laboratory, Tokyo Institute of Technology, Yokohama, Kanagawa 226-8503
Corresponding Author: myoshida{at}res.titech.ac.jp
Coupling of proton flow and rotation in Fo 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 Fo, either in the F1-stripped inverted vesicles or in the reconstituted Fo-proteoliposomes, hardly mediated passive proton translocation through Fo. Careful analysis using single mutants (bL2C or cS2C) as controls indicated that 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; no rotation of the c-ring, no proton flow through Fo.
J. Biol. Chem, 10.1074/jbc.M111210200
Submitted on November 26, 2001
Revised on January 25, 2002
Accepted on January 28, 2002
Fo of ATP synthase is a rotary proton channel: Obligatory coupling of proton translocation with rotation of c-subunit ring
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