X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. Radiodurans phytochrome

Feifei Li; E. Sethe Burgie; Tao Yu; Annie Héroux; George C. Schatz; Richard D. Vierstra; Allen M. Orville

doi:10.1021/ja510923m

X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. Radiodurans phytochrome

Feifei Li, E. Sethe Burgie, Tao Yu, Annie Héroux, George C. Schatz, Richard D. Vierstra, Allen M. Orville

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

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.

Original language	English
Pages (from-to)	2792-2795
Number of pages	4
Journal	Journal of the American Chemical Society
Volume	137
Issue number	8
DOIs	https://doi.org/10.1021/ja510923m
State	Published - Mar 4 2015

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title = "X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. Radiodurans phytochrome",

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.",

author = "Feifei Li and Burgie, {E. Sethe} and Tao Yu and Annie H{\'e}roux and Schatz, {George C.} and Vierstra, {Richard D.} and Orville, {Allen M.}",

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T1 - X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. Radiodurans phytochrome

AU - Li, Feifei

AU - Burgie, E. Sethe

AU - Yu, Tao

AU - Héroux, Annie

AU - Schatz, George C.

AU - Vierstra, Richard D.

AU - Orville, Allen M.

PY - 2015/3/4

Y1 - 2015/3/4

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84924311188&partnerID=8YFLogxK

U2 - 10.1021/ja510923m

DO - 10.1021/ja510923m

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EP - 2795

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 8

ER -

X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. Radiodurans phytochrome

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