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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 May 1;69(Pt 5):506-9. doi: 10.1107/S1744309113006398. Epub 2013 Apr 30.

Expression, purification, crystallization and preliminary X-ray structure analysis of wild-type and L(M196)H-mutant Rhodobacter sphaeroides reaction centres.

Author information

1
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation. azat@vega.protres.ru

Abstract

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.

KEYWORDS:

Rhodobacter sphaeroides; bacteriochlorophyll; photosynthetic reaction centres; primary electron donor; site-directed mutagenesis

PMID:
23695564
PMCID:
PMC3660888
DOI:
10.1107/S1744309113006398
[Indexed for MEDLINE]
Free PMC Article

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