Light-Induced Structural Changes in a Photosynthetic Reaction Center Caught by Laue Diffraction
Artikel i vetenskaplig tidskrift, 2010
Photosynthetic reaction centers convert the energy content of light into a transmembrane potential
difference and so provide the major pathway for energy input into the biosphere. We applied
time-resolved Laue diffraction to study light-induced conformational changes in the photosynthetic
reaction center complex of
Blastochloris viridis. The side chain of TyrL162, which lies adjacent to the
special pair of bacteriochlorophyll molecules that are photooxidized in the primary light conversion event
of photosynthesis, was observed to move 1.3 angstroms closer to the special pair after photoactivation.
Free energy calculations suggest that this movement results from the deprotonation of this conserved
tyrosine residue and provides a mechanism for stabilizing the primary charge separation reactions of
photosynthesis.
SPECIAL PAIR
RHODOBACTER-SPHAEROIDES
CYTOCHROME
RHODOPSEUDOMONAS-VIRIDIS
VIRIDIS REACTION CENTERS
TEMPERATURE
SPECTROSCOPY
PROTEIN
TIME-RESOLVED CRYSTALLOGRAPHY
ELECTRON-TRANSFER
Författare
Annemarie Wöhri
Chalmers, Kemi- och bioteknik, Molekylär mikroskopi
Gergely Katona
Göteborgs universitet
Linda C Johansson
Göteborgs universitet
Emelie Fritz
Göteborgs universitet
Erik Malmerberg
Göteborgs universitet
Magnus Andersson
Chalmers, Kemi- och bioteknik, Molekylär mikroskopi
J Vincent
Uppsala Universitet
Mattias Eklund
Uppsala Universitet
Marco Cammarata
European Synchrotron Radiation Facility
Michael Wulff
Stanford Linear Accelerator Center
European Synchrotron Radiation Facility
J Davidsson
Uppsala Universitet
G. Groenhof
Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute)
Richard Neutze
Göteborgs universitet
Science
0036-8075 (ISSN)
Vol. 328 5978 630-633Ämneskategorier (SSIF 2011)
Kemi
DOI
10.1126/science.1186159