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

@article{Corchnoy2003IntramolecularPT,
  title={Intramolecular proton transfers and structural changes during the photocycle of the LOV2 domain of phototropin 1.},
  author={Stephanie B Corchnoy and Trevor E. Swartz and J. W. Lewis and Istvan Szundi and Winslow R. Briggs and Roberto A. Bogomolni},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 2},
  pages={724-31}
}
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… CONTINUE READING

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