Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 8, Pages 2792-2795Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja510923m
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Funding
- NIH/NIGMS [8P41GM103473-16]
- DOE/BER [FWP BO-70]
- NSF [MCB-1329956]
- Ultrafast Initiative of the U. S. Department of Energy, Office of Science, Office of Basic Energy Sciences through Argonne National Laboratory [DE-AC02-06CH11357]
- U.S. Department of Energy Office of Basic Energy Sciences [DE-AC02-98CH10886]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P41GM103473] Funding Source: NIH RePORTER
- Direct For Biological Sciences [1623935] Funding Source: National Science Foundation
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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.
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