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J. Biol. Chem., Vol. 276, Issue 43, 39505-39507, October 26, 2001
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From In F1-ATPase, the
smallest known motor enzyme, unidirectional rotation of the central
axis subunit
ACCELERATED PUBLICATION
Redox Regulation of the Rotation of
F1-ATP Synthase*
§¶,
,§,, and**
PRESTO, 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
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 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 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 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.
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