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

^*Corresponding author for this work

Chemistry

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

18 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 (US)
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

ASJC Scopus subject areas

General Chemistry
Biochemistry
Catalysis
Colloid and Surface Chemistry

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10.1021/ja510923m

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@article{dacfe5a8af7f4c3c8a64ec5cd409bf24,

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.\}",

note = "Publisher Copyright: {\textcopyright} 2015 American Chemical Society.",

year = "2015",

month = mar,

day = "4",

doi = "10.1021/ja510923m",

language = "English (US)",

volume = "137",

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TY - JOUR

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 - https://www.scopus.com/pages/publications/84924311188

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

U2 - 10.1021/ja510923m

DO - 10.1021/ja510923m

M3 - Article

C2 - 25650486

AN - SCOPUS:84924311188

SN - 0002-7863

VL - 137

SP - 2792

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

Abstract

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PAS-GAF fragment from Deinococcus radiodurans BphP assembled with BV - Y307S, high dose

PAS-GAF fragment from Deinococcus radiodurans BphP assembled with BV - Y307S, low dose

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

Abstract

ASJC Scopus subject areas

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Datasets

PAS-GAF fragment from Deinococcus radiodurans BphP assembled with BV - Y307S, high dose

PAS-GAF fragment from Deinococcus radiodurans BphP assembled with BV - Y307S, low dose

Cite this