Excited-state relaxation dynamics of a PYP chromophore model in solution: influence of the thioester group
Excited-state relaxation dynamics of a PYP chromophore model in solution: influence of the thioester group
复制标题
DOI：
10.1016/s0009-2614(02)01480-x
复制
发表时间：
2002-11-05
影响因子：
2.8
通讯作者：
Martin, MM
中科院分区：
文献类型：
--
作者：
Changenet-Barret, P;Espagne, A;Martin, MM
通过亚皮秒瞬态吸收和增益光谱研究了光活性黄色蛋白发色团模型（去质子化的反式 S-苯硫基-对羟基肉桂酸酯）在水溶液中的顺反光异构化。研究发现，激发态失活涉及在 1.7 ps 内形成中间态，并在 2.8 ps 内衰减。在较长时间内观察到持续的漂白信号，表明激发态不仅弛豫到基态，而且部分形成稳定的光产物，可能是顺式异构体。这种行为类似于天然光敏黄色蛋白的行为。 (C) 2002 Elsevier Science B.V. 保留所有权利。
Cis-trans photoisomerization of a photoactive yellow protein chromophore model, the deprotonated trans S-phenyl thio-p-hydroxycinnamate, is studied in aqueous solution by subpicosecond transient absorption and gain spectroscopy. The excited-state deactivation is found to involve the formation, in 1.7 ps, of an intermediate state which decays in 2.8 ps. A persistent bleaching signal is observed at longer times indicating that the excited state not only relaxes to the ground state but also partly forms a stable photoproduct, possibly the cis isomer. This behavior is analogous to that of the native photoactive yellow protein. (C) 2002 Elsevier Science B.V. All rights reserved.