Ultrafast spectroscopy of biological photoreceptors

被引:89
作者
Kennis, John T. M. [1 ]
Groot, Marie-Louise [1 ]
机构
[1] Vrije Univ Amsterdam, Fac Sci, Dept Biophys, NL-1081 HV Amsterdam, Netherlands
关键词
D O I
10.1016/j.sbi.2007.09.006
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 review recent new insights on reaction dynamics of photoreceptors; proteins gained from ultrafast spectroscopy. In Blue Light sensing Using FAD (BLUF) domains, a hydrogenbond rearrangement around the flavin chromophore proceeds through a radical-pair mechanism, by which light-induced electron and proton transfer from the protein to flavin result in rotation of a conserved glutamine that switches the hydrogen bond network. Femtosecond infrared spectroscopy has shown that in photoactive yellow protein (PYP), breaking of a hydrogen bond that connects the p-coumaric acid chromophore to the backbone is crucial for trans-cis isomerization and successful entry into the photocycle. Furthermore, isomerization reactions of phycocyanobilin in phytochrome and retinal in the rhodopsins have been revealed in detail through application of femtosecond infrared and femtosecond-stimulated Raman spectroscopy.
引用
收藏
页码:623 / 630
页数:8
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