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Title: X-ray Radiation Induces Deprotonation of the Bilin Chromophore in Crystalline D. Radiodurans Phytochrome

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. Furthermore, 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.
 [1] ;  [2] ;  [3] ;  [4] ;  [3] ;  [2] ;  [4]
  1. Brookhaven National Lab. (BNL), Upton, NY (United States); New Mexico State Univ., Las Cruces, NM (United States)
  2. Univ. of Wisconsin, Madison, WI (United States)
  3. Northwestern Univ., Evanston, IL (United States)
  4. Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
OSTI Identifier:
Report Number(s):
Journal ID: ISSN 0002-7863
DOE Contract Number:
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of the American Chemical Society; Journal Volume: 137; Journal Issue: 8
American Chemical Society (ACS)
Research Org:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States