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Role of the Isoprenyl Tail of Ubiquinone in Reaction with Respiratory Enzymes:  Studies with Bovine Heart Mitochondrial Complex I and Escherichiacolibo-Type Ubiquinol Oxidase

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Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan, Central Research Laboratory, Ishihara Sangyo Kaisha Ltd., Kusatsu, Shiga 525-0025, Japan, and Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
Cite this: Biochemistry 1998, 37, 43, 15106–15113
Publication Date (Web):October 9, 1998
Copyright © 1998 American Chemical Society

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    The hydrophobic isoprene tail of ubiquinone-2 (Q2) exihibits binding specificity in redox reactions with bovine heart mitochondrial complex I (Ohshima, M., Miyoshi, H., Sakamoto, K., Takegami, K., Iwata, J., Kuwabara, K., Iwamura, H., and Yagi, T. (1998) Biochemistry37, 6436−6445) and the Escherichiacolibo-type ubiquinol oxidase (Sakamoto, K., Miyoshi, H., Takegami, K., Mogi, T., Anraku, Y., and Iwamura, H. (1996) J.Biol.Chem.271, 29897−29902). To identify the structural factor(s) of the diprenyl tail of Q2 governing the specific interaction with these enzymes, we synthesized a series of novel Q2 analogues in which only one of the structural factors of the diprenyl tail was systematically modified. In bovine complex I, the presence of the methyl branch and the π-electron system in the first isoprene unit are responsible for high-affinity binding of Q2 to the ubiquinone reduction site, which results in a low Km and kcat values of Q2 reduction. The position of the methyl group in the tail is strictly recognized by the enzyme. In contrast to complex I, in bo-type ubiquinol oxidase, either of the two π-electron systems in the tail is required for high-affinity binding of Q2H2 to the enzyme, while the presence of the methyl branch and the location of the π-electron systems are not strictly recognized by the enzyme. We concluded that the role of the ubiquinone tail is not simply the enhancement of the hydrophobicity of the molecule and that molecular recognition of the tail by the quinone redox site differs among the respiratory enzymes.

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     This work was supported in part by Grants-in-Aid for JSPS Fellows (9307 to K.S.), Scientific Research (08660136 to H.M.), and Scientific Research on Priority Areas (08249106 (Molecular Biometallics) to T.M.) from the Ministry of Education, Science, Sports and Culture of Japan.

     Kyoto University.


     To whom correspondence should be addressed. Fax:  +81-75-753-6408. Tel:  +81-75-753-6119. E-mail:  [email protected].


     Ishihara Sangyo Kaisha Ltd.

     University of Tokyo.

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