Initial steps of signal generation in photoactive yellow protein revealed with femtosecond mid-infrared spectroscopy

被引:110
作者
Groot, ML
van Wilderen, LJGW
Larsen, DS
van der Horst, MA
van Stokkum, IHM
Hellingwerf, KJ
van Grondelle, R
机构
[1] Vrije Univ Amsterdam, Fac Sci, NL-1081 HV Amsterdam, Netherlands
[2] Univ Amsterdam, Microbiol Lab, Swammerdam Inst Life Sci, NL-1010 WV Amsterdam, Netherlands
关键词
D O I
10.1021/bi034878p
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
Photoactive yellow protein (PYP) is a bacterial blue light sensor that induces Halorhodospira halophila to swim away from intense blue light. Light absorption by PYP's intrinsic chromophore, p-coumaric acid, leads to the initiation of a photocycle that comprises several distinct intermediates. Here we describe the initial structural changes of the chromophore and its nearby amino acids, using visible pump/mid-infrared probe spectroscopy. Upon photoexcitation, the trans bands of the chromophore are bleached, and shifts of the phenol ring bands occur. The latter are ascribed to charge translocation, which probably plays an essential role in driving the trans to cis isomerization process. We conclude that breaking of the hydrogen bond of the chromophore's C=O group with amino acid Cys69 and formation of a stable cis ground state occur in similar to2 ps. Dynamic changes also include rearrangements of the hydrogen-bonding network of the amino acids around the chromophore. Relaxation of the coumaryl tail of the chromophore occurs in 0.9-1 ns, which event we identify with the I-0 to I-1 transition observed in visible spectroscopy.
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收藏
页码:10054 / 10059
页数:6
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