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Role of protein in the primary step of the photoreaction of yellow protein
Author(s) -
Yamada Atsushi,
Ishikura Takakazu,
Yamato Takahisa
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20006
Subject(s) - chromophore , isomerization , chemistry , photochemistry , excited state , relaxation (psychology) , protein dynamics , computational chemistry , molecular dynamics , organic chemistry , catalysis , physics , psychology , social psychology , nuclear physics
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. Proteins 2004. © 2004 Wiley‐Liss, Inc.

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