Role of arginine 52 on the primary photoinduced events in the PYP photocycle

被引：35

作者：

Changenet-Barret, Pascale

Plaza, Pascal

Martin, Monique M.

Chosrowjan, Haik

Taniguchi, Seiji

Mataga, Noboru

Imamoto, Yasushi

Kataoka, Mikio

机构：

[1] Ecole Normale Super, UMR CNRS 8640, Dept Chim, F-75231 Paris 05, France

[2] ILT, Nishi Ku, Osaka 5500004, Japan

[3] Nara Inst Sci & Technol, Grad Sch Mat Sci, Nara 6300192, Japan

来源：

CHEMICAL PHYSICS LETTERS | 2007年 / 434卷 / 4-6期

关键词：

D O I：

10.1016/j.cplett.2006.12.027

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We investigated the earliest steps of the photocycle of photoactive yellow protein (PYP) and its R52Q mutant in aqueous solution, by subpicosecond transient absorption spectroscopy. Our aim was to address the role of the positively charged Arg52 residue. We found that the relaxation mechanism of R52Q is similar to that of wt-PYP and discarded that Arg52 plays a key role in the chromophore photoreactivity. The excited-state decay of R52Q is however slower, confirming previous fluorescence up-conversion data. The experiments also reveal a slower stabilization of the cis isomer product. The loosening of the protein pocket and structural heterogeneities are discussed. (c) 2006 Elsevier B.V. All rights reserved.

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页码：320 / 325

页数：6

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