Journal
PHOTOSYNTHESIS RESEARCH
Volume 98, Issue 1-3, Pages 365-389Publisher
SPRINGER
DOI: 10.1007/s11120-008-9353-7
Keywords
Photosystem II; Manganese stabilizing protein; Oxygen evolution; Thermophile
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Funding
- Australian Research Council [DP0450421]
- Australian Postgraduate Award
- William Georgetti Scholarship
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The Manganese Stabilizing Protein (MSP) of Photosystem II (PSII) is a so-called extrinsic subunit, which reversibly associates with the other membrane-bound PSII subunits. The MSP is essential for maximum rates of O-2 production under physiological conditions as stabilizes the catalytic [Mn4Ca] cluster, which is the site of water oxidation. The function of the MSP subunit in the PSII complex has been extensively studied in higher plants, and the structure of non-PSII associated MSP has been studied by low-resolution biophysical techniques. Recently, crystal structures of PSII from the thermophilic cyanobacterium Thermosynechococcus elongatus have resolved the MSP subunit in its PSII-associated state. However, neither any crystal structure is available yet for MSP from mesophilic organisms, higher plants or algae nor has the non-PSII associated form of MSP been crystallized. This article reviews the current understanding of the structure, dynamics, and function of MSP, with a particular focus on properties of the MSP from T. elongatus that may be attributable to the thermophilic ecology of this organism rather than being general features of MSP.
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