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Originally published In Press as doi:10.1074/jbc.M209119200 on October 30, 2002

J. Biol. Chem., Vol. 278, Issue 2, 724-731, January 10, 2003
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Intramolecular Proton Transfers and Structural Changes during the Photocycle of the LOV2 Domain of Phototropin 1*

Stephanie B. CorchnoyDagger , Trevor E. Swartz§, James W. LewisDagger , Istvan SzundiDagger , Winslow R. Briggs§, and Roberto A. BogomolniDagger

From the Dagger  Department of Chemistry and Biochemistry, University of California, Santa Cruz, California 95064 and the § Department of Plant Biology, Carnegie Institution of Washington, Stanford, California 94305

The phototropins are a family of membrane-associated flavoproteins that function as the primary blue light receptors regulating phototropism, chloroplast movements, stomatal opening, and leaf expansion in plants. Phot1, a member of this family, contains two FMN-binding domains, LOV1 and LOV2, within the N-terminal region and a C-terminal serine-threonine protein kinase domain. Light irradiation of oat phot1 LOV2 produces a cysteinyl adduct (Cys-39) at the flavin C(4a) position, which decays thermally back to the dark state. We measured pH and isotope effects on the photocycle. Between pH 3.7 and 9.5, adduct formation showed minimal pH dependence, and adduct decay showed only slight pH dependence, indicating that the pK values of mechanistically relevant groups are outside this range. LOV2 showed a nearly 5-fold slowing of adduct formation in D2O relative to H2O, indicating that the rate-limiting step involves proton transfer(s). Light-induced changes in the far UV CD spectrum of LOV2 revealed putative protein structural perturbations. The light minus dark CD difference spectrum resembles an inverted alpha -helix spectrum, suggesting that alpha -helicity is reversibly lost upon light irradiation. Decay kinetics for CD spectral changes in the far UV region occur at the same rate as those in the visible region, indicating synchronous relaxation of protein and chromophore structures.

* This work was supported by faculty research funds granted by the University of California, Santa Cruz (to R. A. B.), research funds provided by Covalent Partners LLC (to R. A. B. and S. B. C.), and National Science Foundation Grants IBN9940546 and MSB-0091384 (to W. R. B.) and DMB-0090817 (to R. A. B.).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.

To whom correspondence should be addressed: Dept. of Chemistry and Biochemistry, University of California, Santa Cruz, 1156 High St., Santa Cruz, CA 95064. Tel.: 831-459-4294; Fax: 831-459-2935; E-mail: bogo@chemistry.ucsc.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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