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X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome.
Li, Feifei; Burgie, E Sethe; Yu, Tao; Héroux, Annie; Schatz, George C; Vierstra, Richard D; Orville, Allen M.
Affiliation
  • Li F; Photon Sciences Directorate and ∥Biosciences Department, Brookhaven National Laboratory , Upton, New York 11973, United States.
J Am Chem Soc ; 137(8): 2792-5, 2015 Mar 04.
Article in En | MEDLINE | ID: mdl-25650486
ABSTRACT
We report that in the red light-absorbing (Pr) state, the bilin chromophore of the Deinococcus radiodurans proteobacterial phytochrome (DrBphP) is hypersensitive to X-ray photons used in typical synchrotron X-ray protein crystallography experiments. This causes the otherwise fully protonated chromophore to deprotonate without additional major structural changes. These results have major implications for our understanding of the structural and chemical characteristics of the resting and intermediate states of phytochromes and other photoreceptor proteins.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phytochrome / Protons / Bacterial Proteins / Bile Pigments / Deinococcus Language: En Journal: J Am Chem Soc Year: 2015 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Phytochrome / Protons / Bacterial Proteins / Bile Pigments / Deinococcus Language: En Journal: J Am Chem Soc Year: 2015 Document type: Article Affiliation country: United States