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Light-Induced Structural Changes in a Photosynthetic Reaction Center Caught by Laue Diffraction

Annemarie Wöhri (Institutionen för kemi- och bioteknik, Molekylär mikroskopi) ; Gergely Katona ; Linda C Johansson ; Emelie Fritz ; Erik Malmerberg ; Magnus Andersson (Institutionen för kemi- och bioteknik, Molekylär mikroskopi) ; J. Vincent ; M. Eklund ; M. Cammarata ; M. Wulff ; J. Davidsson ; G. Groenhof ; Richard Neutze
Science (0036-8075). Vol. 328 (2010), 5978, p. 630-633.
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: TIME-RESOLVED CRYSTALLOGRAPHY, VIRIDIS REACTION CENTERS, RHODOPSEUDOMONAS-VIRIDIS, RHODOBACTER-SPHAEROIDES, ELECTRON-TRANSFER, SPECIAL PAIR, PROTEIN, CYTOCHROME, SPECTROSCOPY, TEMPERATURE



Denna post skapades 2010-05-12. Senast ändrad 2016-10-14.
CPL Pubid: 121554

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Molekylär mikroskopi (2008-2014)
Institutionen för kemi (2001-2011)

Ämnesområden

Kemi

Chalmers infrastruktur