Role of protein in the primary step of the photoreaction of yellow protein

被引：35

作者：

Yamada, A ^{[1
]}

Ishikura, T ^{[1
]}

Yamato, T ^{[1
]}

机构：

[1] Nagoya Univ, Grad Sch Sci, Chikusa Ku, Nagoya, Aichi 4648602, Japan

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2004年 / 55卷 / 04期

关键词：

protein-chromophore interaction; p-coumaric acid; photoisomerization; ONIOM method; driving force; reaction coordinate; chromophore; Photoactive Yellow Protein;

D O I：

10.1002/prot.20006

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We show the unexpectedly important role of the protein environment in the primary step of the photoreaction of the yellow protein after light illumination. The driving force of the trans-to-cis isomerization reaction was analyzed by a computational method. The force was separated into two different components: the term due to the protein-chromophore interaction and the intrinsic term of the chromophore itself. As a result, we found that the contribution from the interaction term was much greater than that coming from the intrinsic term. This accounts for the efficiency of the isomerization reaction in the protein environment in contrast to that in solution environments. We then analyzed the relaxation process of the chromophore on the excited-state energy surface and compared the process in the protein environment and that in a vacuum. Based on this analysis, we found that the bond-selectivity of the isomerization reaction also comes from the interaction between the chromophore and the protein environment. (C) 2004 Wiley-Liss, Inc.

引用

页码：1063 / 1069

页数：7