Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1817, Issue 1, Pages 121-142Publisher
ELSEVIER
DOI: 10.1016/j.bbabio.2011.07.006
Keywords
PsbO; PsbP; PsbQ; PsbU; PsbV
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Funding
- United States Department of Energy [DE-FG02-98ER20310]
- USDA National Institute of Food and Agriculture [2008-35318-04605]
- Marsden Grant [08-UOO-043]
- U.S. Department of Energy (DOE) [DE-FG02-98ER20310] Funding Source: U.S. Department of Energy (DOE)
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In this review we examine the structure and function of the extrinsic proteins of Photosystem II. These proteins include PsbO, present in all oxygenic organisms, the PsbP and PsbQ proteins, which are found in higher plants and eukaryotic algae, and the PsbU, PsbV, CyanoQ and CyanoP proteins, which are found in the cyanobacteria. These proteins serve to optimize oxygen evolution at physiological calcium and chloride concentrations. They also shield the Mn4CaO5 cluster from exogenous reductants. Numerous biochemical, genetic and structural studies have been used to probe the structure and function of these proteins within the photosystem. We will discuss the most recent proposed functional roles for these components, their structures (as deduced from biochemical and X-ray crystallographic studies) and the locations of their proposed binding domains within the Photosystem II complex. This article is part of a Special Issue entitled: Photosystem II. (C) 2011 Elsevier B.V. All rights reserved.
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