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J. Biol. Chem., Vol. 280, Issue 43, 36237-36243, October 28, 2005

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Identification and Characterization of a Second Chromophore of DNA Photolyase from Thermus thermophilus HB27^*

Takumi Ueda, Akira Kato, Seiki Kuramitsu¶, Hiroaki Terasawa, and Ichio Shimada||1

From the Graduate School of Pharmaceutical Sciences, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, the Japan Biological Information Research Center, Japan Biological Informatics Consortium, Hatchobori, Chuo-ku, Tokyo 104-0032, Japan, the ^¶Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan, and the ^||Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, Aomi, Koto-ku, Tokyo 135-0064, Japan

Cyclobutane pyrimidine dimer (CPD) photolyases use light to repair CPDs. For efficient light absorption, CPD photolyases use a second chromophore. We purified Thermus thermophilus CPD photolyase with its second chromophore. UV-visible absorption spectra, reverse-phase HPLC, and NMR analyses of the chromophores revealed that the second chromophore of the enzyme is flavin mononucleotide (FMN). To clarify the role of FMN in the CPD repair reaction, the enzyme without FMN (Enz-FMN(-) and that with a stoichiometric amount of FMN (Enz-FMN(+)) were both successfully obtained. The CPD repair activity of Enz-FMN(+) was higher than that of Enz-FMN(-), and the CPD repair activity ratio of Enz-FMN(+) and Enz-FMN(-) was dependent on the wavelength of light. These results suggest that FMN increases the light absorption efficiency of the enzyme. NMR analyses of Enz-FMN(+) and Enz-FMN(-) revealed that the binding mode of FMN is similar to that of 7,8-didemethyl-8-hydroxy-5-deazariboflavin in Anacystis nidulans CPD photolyase, and thus a direct electron transfer between FMN and CPD is not likely to occur. Based on these results, we concluded that FMN acts as a highly efficient light harvester that gathers light and transfers the energy to FAD.

Received for publication, July 21, 2005 , and in revised form, August 22, 2005.

^* This work was supported by grants from the Japan New Energy and Industrial Technology Development Organization and the Ministry of Economy, Trade, and Industry. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Graduate School of Pharmaceutical Sciences, the University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Tel. and Fax: 81-3-3815-6540; E-mail: shimada{at}iw-nmr.f.u-tokyo.ac.jp.

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