Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Science Careers Booklet

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 20 March 1998:
Vol. 279. no. 5358, pp. 1946 - 1950
DOI: 10.1126/science.279.5358.1946
Prev | Table of Contents | Next

Reports

Energy Transduction on the Nanosecond Time Scale: Early Structural Events in a Xanthopsin Photocycle

Benjamin Perman, Vukica Šrajer, Zhong Ren, Tsu-yi Teng, Claude Pradervand, Thomas Ursby, Dominique Bourgeois, Friederich Schotte, Michael Wulff, Remco Kort, Klaas Hellingwerf, Keith Moffat *

Photoactive yellow protein (PYP) is a member of the xanthopsin family of eubacterial blue-light photoreceptors. On absorption of light, PYP enters a photocycle that ultimately transduces the energy contained in a light signal into an altered biological response. Nanosecond time-resolved x-ray crystallography was used to determine the structure of the short-lived, red-shifted, intermediate state denoted [pR], which develops within 1 nanosecond after photoelectronic excitation of the chromophore of PYP by absorption of light. The resulting structural model demonstrates that the [pR] state possesses the cis conformation of the 4-hydroxyl cinnamic thioester chromophore, and that the process of trans to cis isomerization is accompanied by the specific formation of new hydrogen bonds that replace those broken upon excitation of the chromophore. Regions of flexibility that compose the chromophore-binding pocket serve to lower the activation energy barrier between the dark state, denoted pG, and [pR], and help initiate entrance into the photocycle. Direct structural evidence is provided for the initial processes of transduction of light energy, which ultimately translate into a physiological signal.

B. Perman, Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
V. Šrajer, Z. Ren, T.-y. Teng, C. Pradervand, K. Moffat, Department of Biochemistry and Molecular Biology and the Consortium for Advanced Radiation Sources, University of Chicago, Chicago, IL 60637, USA.
T. Ursby, Molecular Biophysics, Chemical Center, Lund University, Post Office Box 124, S-221 00 Lund, Sweden.
D. Bourgeois, F. Schotte, M. Wulff, European Synchrotron Radiation Facility, 38043 Grenoble Cedex, France.
R. Kort and K. Hellingwerf, Laboratory for Microbiology, E. C. Slater Institute, 1018 WS Amsterdam, Netherlands.
*   To whom correspondence should be addressed. E-mail: moffat{at}cars.uchicago.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Ultrafast infrared spectroscopy reveals a key step for successful entry into the photocycle for photoactive yellow protein.
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 (2006)
PNAS 103, 15050-15055
   Abstract »    Full Text »    PDF »
Absorption Spectra of Photoactive Yellow Protein Chromophores in Vacuum.
I. B. Nielsen, S. Boye-Peronne, M. O. A. El Ghazaly, M. B. Kristensen, S. Brondsted Nielsen, and L. H. Andersen (2005)
Biophys. J. 89, 2597-2604
   Abstract »    Full Text »    PDF »
From The Cover: Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds.
H. Ihee, S. Rajagopal, V. Srajer, R. Pahl, S. Anderson, M. Schmidt, F. Schotte, P. A. Anfinrud, M. Wulff, and K. Moffat (2005)
PNAS 102, 7145-7150
   Abstract »    Full Text »    PDF »
Predicting the Signaling State of Photoactive Yellow Protein.
J. Vreede, W. Crielaard, K. J. Hellingwerf, and P. G. Bolhuis (2005)
Biophys. J. 88, 3525-3535
   Abstract »    Full Text »    PDF »
Contrasting the Excited-State Dynamics of the Photoactive Yellow Protein Chromophore: Protein versus Solvent Environments.
M. Vengris, M. A. van der Horst, G. Zgrablic, I. H. M. van Stokkum, S. Haacke, M. Chergui, K. J. Hellingwerf, R. van Grondelle, and D. S. Larsen (2004)
Biophys. J. 87, 1848-1857
   Abstract »    Full Text »    PDF »
Incoherent Manipulation of the Photoactive Yellow Protein Photocycle with Dispersed Pump-Dump-Probe Spectroscopy.
D. S. Larsen, I. H. M. van Stokkum, M. Vengris, M. A. van der Horst, F. L. de Weerd, K. J. Hellingwerf, and R. van Grondelle (2004)
Biophys. J. 87, 1858-1872
   Abstract »    Full Text »    PDF »
Initial Events in the Photocycle of Photoactive Yellow Protein.
R. Kort, K. J. Hellingwerf, and R. B. G. Ravelli (2004)
J. Biol. Chem. 279, 26417-26424
   Abstract »    Full Text »    PDF »
Protein kinetics: Structures of intermediates and reaction mechanism from time-resolved x-ray data.
M. Schmidt, R. Pahl, V. Srajer, S. Anderson, Z. Ren, H. Ihee, S. Rajagopal, and K. Moffat (2004)
PNAS 101, 4799-4804
   Abstract »    Full Text »    PDF »
Photoisomerization and Photoionization of the Photoactive Yellow Protein Chromophore in Solution.
D. S. Larsen, M. Vengris, I. H. M. van Stokkum, M. A. van der Horst, F. L. de Weerd, K. J. Hellingwerf, and R. van Grondelle (2004)
Biophys. J. 86, 2538-2550
   Abstract »    Full Text »    PDF »
Deformation of Helix C in the Low Temperature L-intermediate of Bacteriorhodopsin.
K. Edman, A. Royant, G. Larsson, F. Jacobson, T. Taylor, D. van der Spoel, E. M. Landau, E. Pebay-Peyroula, and R. Neutze (2004)
J. Biol. Chem. 279, 2147-2158
   Abstract »    Full Text »    PDF »
PAS Domains. COMMON STRUCTURE AND COMMON FLEXIBILITY.
J. Vreede, M. A. van der Horst, K. J. Hellingwerf, W. Crielaard, and D. M. F. van Aalten (2003)
J. Biol. Chem. 278, 18434-18439
   Abstract »    Full Text »    PDF »
Application of Singular Value Decomposition to the Analysis of Time-Resolved Macromolecular X-Ray Data.
M. Schmidt, S. Rajagopal, Z. Ren, and K. Moffat (2003)
Biophys. J. 84, 2112-2129
   Abstract »    Full Text »    PDF »
Crystal structure of a photoactive yellow protein from a sensor histidine kinase: Conformational variability and signal transduction.
S. Rajagopal and K. Moffat (2003)
PNAS 100, 1649-1654
   Abstract »    Full Text »    PDF »
Deuterium Isotope Effects in the Photocycle Transitions of the Photoactive Yellow Protein.
J. Hendriks, I. H. M. van Stokkum, and K. J. Hellingwerf (2003)
Biophys. J. 84, 1180-1191
   Abstract »    Full Text »    PDF »
Structures of bromoalkanes' photodissociation in solution by means of ultrafast extended x-ray absorption fine-structure spectroscopy.
D. A. Oulianov, I. V. Tomov, A. S. Dvornikov, and P. M. Rentzepis (2002)
PNAS 99, 12556-12561
   Abstract »    Full Text »    PDF »
Engineering Photocycle Dynamics. CRYSTAL STRUCTURES AND KINETICS OF THREE PHOTOACTIVE YELLOW PROTEIN HINGE-BENDING MUTANTS.
D. M. F. van Aalten, A. Haker, J. Hendriks, K. J. Hellingwerf, L. Joshua-Tor, and W. Crielaard (2002)
J. Biol. Chem. 277, 6463-6468
   Abstract »    Full Text »    PDF »
Folding and signaling share the same pathway in a photoreceptor.
B.-C. Lee, A. Pandit, P. A. Croonquist, and W. D. Hoff (2001)
PNAS
   Abstract »    Full Text »    PDF »
On the absorbance changes in the photocycle of the photoactive yellow protein: A quantum-chemical analysis.
V. Molina and M. Merchán (2001)
PNAS
   Abstract »    Full Text »
Protonation/Deprotonation Reactions Triggered by Photoactivation of Photoactive Yellow Protein from Ectothiorhodospira halophila.
J. Hendriks, W. D. Hoff, W. Crielaard, and K. J. Hellingwerf (1999)
J. Biol. Chem. 274, 17655-17660
   Abstract »    Full Text »    PDF »
Shedding light on the dark and weakly fluorescent states of green fluorescent proteins.
W. Weber, V. Helms, J. A. McCammon, and P. W. Langhoff (1999)
PNAS 96, 6177-6182
   Abstract »    Full Text »    PDF »
Ultrafast electron diffraction and direct observation of transient structures in a chemical reaction.
J. Cao, H. Ihee, and A. H. Zewail (1999)
PNAS 96, 338-342
   Abstract »    Full Text »    PDF »
trans/cis (Z/E) photoisomerization of the chromophore of photoactive yellow protein is not a prerequisite for the initiation of the photocycle of this photoreceptor protein.
R. Cordfunke, R. Kort, A. Pierik, B. Gobets, G.-J. Koomen, J. W. Verhoeven, and K. J. Hellingwerf (1998)
PNAS 95, 7396-7401
   Abstract »    Full Text »    PDF »
Chemical Dynamics in Proteins: The Photoisomerization of Retinal in Bacteriorhodopsin.
F. Gai, K. C. Hasson, J. C. McDonald, and P. A. Anfinrud (1998)
Science 279, 1886-1891
   Abstract »    Full Text »
PAS Domain Receptor Photoactive Yellow Protein Is Converted to a Molten Globule State upon Activation.
B.-C. Lee, P. A. Croonquist, T. R. Sosnick, and W. D. Hoff (2001)
J. Biol. Chem. 276, 20821-20823
   Abstract »    Full Text »    PDF »
Mimic of Photocycle by a Protein Folding Reaction in Photoactive Yellow Protein.
B.-C. Lee, P. A. Croonquist, and W. D. Hoff (2001)
J. Biol. Chem. 276, 44481-44487
   Abstract »    Full Text »    PDF »
On the absorbance changes in the photocycle of the photoactive yellow protein: A quantum-chemical analysis.
V. Molina and M. Merchan (2001)
PNAS 98, 4299-4304
   Abstract »    Full Text »    PDF »
Folding and signaling share the same pathway in a photoreceptor.
B.-C. Lee, A. Pandit, P. A. Croonquist, and W. D. Hoff (2001)
PNAS 98, 9062-9067
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)