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Biophys. J. BioFAST: First Published March 2, 2006. doi:10.1529/biophysj.105.074765
© 2006 by the Biophysical Society.

A more recent version of this article appeared on June 1, 2006.
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SPECTROSCOPY, IMAGING, OTHER TECHNIQUES

Influence of the crystalline state on photo-induced dynamics of Photoactive Yellow Protein studied by UV/Vis transient absorption spectroscopy

Sergey Yeremenko 1, Ivo H. M. van Stokkum 2, Keith Moffat 3 and Klaas J. Hellingwerf 4*

1 AMOLF
2 Vrije Universiteit van Amsterdam
3 University of Chicago
4 Swammerdam Institute for Lifesciences, University of Amsterdam

* To whom correspondence should be addressed. E-mail: k.hellingwerf{at}science.uva.nl.

Submitted on September 19, 2005
Revised on January 6, 2006
Accepted on 26 January 2006


  Abstract
Time-resolved UV/Vis spectroscopy was used to characterize the photocycle transitions in single crystals of wild-type and the E46Q mutant of Photoactive Yellow Protein (PYP), with microsecond time resolution. The results were compared with the results of similar measurements on aqueous solutions of these two variants of PYP, with and without the components present in the mother liquor of crystals. The experimental data were analyzed with global and target analysis. Distinct differences in the reaction path of a PYP molecule are observed between these conditions, when it progresses through its photocycle. In the crystalline state: (i) much faster relaxation of the late blue-shifted photocycle intermediate back to the ground state is observed, (ii) this intermediate in crystalline PYP absorbs at 380 nm, rather than at 350 to 360 nm in solution, and(iii) for various intermediates of this photocycle the forward reaction through the photocycle directly competes with a branching reaction that leads directly to the ground state. Significantly, with these altered characteristics, the spectroscopic data on PYP are fully consistent with the structural data obtained for this photoreceptor protein with time-resolved X-ray diffraction analysis, particularly for wild-type PYP.

Key Words: macro-molecular crowding, photocycle mechanism, single crystal UV/Vis spectroscopy, target analysis




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 Proc. Natl. Acad. Sci. USAHome page
L. J. G. W. van Wilderen, M. A. van der Horst, I. H. M. van Stokkum, K. J. Hellingwerf, R. van Grondelle, and M. L. Groot
Ultrafast infrared spectroscopy reveals a key step for successful entry into the photocycle for photoactive yellow protein
PNAS, October 10, 2006; 103(41): 15050 - 15055.
[Abstract] [Full Text] [PDF]


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Copyright © 2006 by the Biophysical Society.