Changes in the Hydrogen-Bond Network around the Chromophore of Photoactive Yellow Protein in the Ground and Excited States

被引:26
|
作者
Mizuno, Misao [1 ]
Kamikubo, Hironari [2 ]
Kataoka, Mikio [2 ]
Mizutani, Yasuhisa [1 ]
机构
[1] Osaka Univ, Grad Sch Sci, Dept Chem, Osaka 5600043, Japan
[2] Nara Inst Sci & Technol, Grad Sch Mat Sci, Nara 6300192, Japan
关键词
RESONANCE RAMAN-SPECTROSCOPY; ECTOTHIORHODOSPIRA-HALOPHILA; TYROSINE; ISOMERIZATION; ENVIRONMENT; DEPENDENCE; EVOLUTION; RESIDUES; DYNAMICS; SITE;
D O I
10.1021/jp2029399
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
Changes in the hydrogen-bond (HB) network around the chromophore, p-coumaric acid (pCA), in the ground pG and excited pG* states were investigated for wild type (WT) photoactive yellow protein (PYP) and its mutants using ultraviolet resonance Raman (UVRR) spectroscopy. The intensity depletion of Tyr UVRR bands was observed upon photoexcitation of pCA to the pG* state. The spectral change was ascribed to strengthening of HB between pCA and, Tyr42. Comparison of Raman intensities indicated that, in the pG state, the HB between pCA and Tyr42 in WT is a short HB, which is weaker than that in E46Qmutant. In the pG* state, the HB network around pCA of WT is similar to that of E46Qmutant. The present results demonstrate that the HB between pCA and Tyr42 and that between pCA and Glu46 are correlated with each other in the HB network.
引用
收藏
页码:9306 / 9310
页数:5
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