Open AccessExpression, purification, crystallization and preliminary X‐ray structure analysis of wild‐type and L(M196)H‐mutant Rhodobacter sphaeroides reaction centres
Author(s) -
Gabdulkhakov A. G.,
Fufina T. Y.,
Vasilieva L. G.,
Mueller U.,
Shuvalov V. A.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113006398
Subject(s) - rhodobacter sphaeroides , periplasmic space , mutant , photosynthetic reaction centre , rhodospirillaceae , chemistry , photosynthesis , rhodospirillales , electron transfer , crystallization , electron transport chain , wild type , electrochemical gradient , proton , crystallography , photochemistry , membrane , biochemistry , escherichia coli , physics , organic chemistry , quantum mechanics , gene
The electron and proton transport mediated by protein‐bound cofactors in photosynthesis have been investigated by various methods in order to determine the energetics, the dynamics and the pathway of this process. In purple bacteria, primary photosynthetic charge separation and the build‐up of a proton gradient across the periplasmic membrane are catalyzed by the photosynthetic reaction centre (RC). Here, the purification, crystallization and preliminary X‐ray analysis of wild‐type and L(M196)H‐mutant RCs of Rhodobacter sphaeroides are presented, enabling study of the influence of the protein environment of the primary electron donor on the spectral properties and photochemical activity of the RC.