کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1942344 | 1052607 | 2012 | 22 صفحه PDF | دانلود رایگان |

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.
► We have reviewed the structure and function of the extrinsic proteins of PS II.
► The differences between the higher plant and cyanobacterial systems are examined.
► Putative docking sites of the CyanoQ and CyanoP proteins onto PS II are proposed.
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1817, Issue 1, January 2012, Pages 121–142