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Originally published In Press as doi:10.1074/jbc.C100436200 on August 22, 2001

J. Biol. Chem., Vol. 276, Issue 43, 39505-39507, October 26, 2001
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ACCELERATED PUBLICATION
Redox Regulation of the Rotation of F1-ATP Synthase*

Dirk BaldDagger §, Hiroyuki Noji||, Masasuke YoshidaDagger §, Yoko Hirono-HaraDagger , and Toru HisaboriDagger **

From || PRESTO, Dagger  Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama, Kanagawa 226-8503 and § CREST Genetic Programming Team 13, Teikyo University Biotechnology Research Center 3F, Nogawa 907, Miyamae-ku, Kawasaki, Kanagawa 216-0001, Japan

In F1-ATPase, the smallest known motor enzyme, unidirectional rotation of the central axis subunit gamma  is coupled to ATP hydrolysis. In the present study, we report the redox switching of the rotation of this enzyme. For this purpose, the switch region from the gamma  subunit of the redox-sensitive chloroplast F1-ATPase was introduced into the bacterial F1-ATPase. The ATPase activity of the obtained complex was increased up to 3-fold upon reduction (Bald, D., Noji, H., Stumpp, M. T., Yoshida, M. & Hisabori, T. (2000) J. Biol. Chem. 275, 12757-12762). Here, we successfully observed the modulation of rotation of gamma  in this chimeric complex by changes in the redox conditions. In addition we revealed that the suppressed enzymatic activity of the oxidized F1-ATPase complex was characterized by more frequent long pauses in the rotation of the gamma  subunit. These findings obtained by the single molecule analysis therefore provide new insights into the mechanisms of enzyme regulation.

* This work was supported in part by CREST Genetic Programming Team 13, Japan Science and Technology Corporation (to M. Y.) and by Grants-in-aid 11151209 and 12025207 for scientific research on priority areas (A) (to T. H.) from the Ministry of Education, Sports, Science and Technology of Japan, and by a research fellowship from the Japan Society for the Promotion of Science (to Y. H.-H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Dept. of Structural Biology, Free University of Amsterdam, De Boelelaan 1087, 1081 Amsterdam, Netherlands.

** To whom correspondence should be addressed. E-mail: thisabor@res.titech.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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