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.

TIME-RESOLVED CRYSTALLOGRAPHY

PROTEIN

VIRIDIS REACTION CENTERS

CYTOCHROME

RHODOBACTER-SPHAEROIDES

RHODOPSEUDOMONAS-VIRIDIS

TEMPERATURE

SPECIAL PAIR

ELECTRON-TRANSFER

SPECTROSCOPY

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 (ESRF)

Michael Wulff

European Synchrotron Radiation Facility (ESRF)

Stanford Linear Accelerator Center

J Davidsson

Uppsala universitet

G. Groenhof

Max Planck-institutet

Richard Neutze

Göteborgs universitet

Science

0036-8075 (ISSN)

Vol. 328 630-633

Ämneskategorier

Kemi

DOI

10.1126/science.1186159