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M209119200v1
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Papers In Press, published online ahead of print October 30, 2002
J. Biol. Chem, 10.1074/jbc.M209119200
Submitted on September 6, 2002
Revised on October 29, 2002
Accepted on October 30, 2002

Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1

Stephanie B. Corchnoy, Trevor E. Swartz, James W. Lewis, Istvan Szundi, Winslow R. Briggs, and Roberto A. Bogomolni

Chemistry and Biochemistry, University of California at Santa Cruz, Santa Cruz, California 95064

Corresponding Author: bogo{at}chemistry.ucsc.edu

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 FMN1-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 (cys39)2 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 five-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 circular dichroism (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.


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