The D1 and D2 Core Proteins

Nixon, Peter J.; Sarcina, Mary; Diner, Bruce A.

doi:10.1007/1-4020-4254-x_5

Cited by 13 publications

(45 citation statements)

References 201 publications

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“…D1 and D2 bind all the redox-active cofactors of the acceptor-side electron transport chain. D1 and CP43 bind the [Mn 4 Ca] metal cluster of the OEC (Nixon et al 2005). The extrinsic proteins function to stabilize the OEC and provide the correct environment for its optimal function (Bricker and Burnap 2005).…”

Section: An Overview Of the Psii Manganese Stabilizing Proteinmentioning

confidence: 99%

Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms

Williamson

2008

Photosynth Res

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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 [Mn(4)Ca] 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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Section: An Overview Of the Psii Manganese Stabilizing Proteinmentioning

confidence: 99%

Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms

Williamson

2008

Photosynth Res

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“…It is made up of a number of intrinsic trans-membrane proteins and between 1 and 5 extrinsic proteins depending on the species (Seidler 1996;Nixon et al 2005;Eaton-Rye and Putnam-Evans 2005;Loll et al 2005b and references therein). The extrinsic proteins, along with luminal portions of the intrinsic proteins and an inorganic metal cluster make up a domain of PSII termed the water oxidizing complex (WOC) where oxygen is produced.…”

Section: Introductionmentioning

confidence: 99%

The importance of protein–protein interactions for optimising oxygen activity in photosystem II: reconstitution with a recombinant thioredoxin—manganese stabilising protein

et al. 2007

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In this paper we describe how photosystem II (PSII) from higher plants, which have been depleted, of the extrinsic proteins can be reconstituted with a chimeric fusion protein comprising thioredoxin from Escherichia coli and the manganese stabilising protein from Thermosynechococcus elongatus. Surprisingly, even though E. coli thioredoxin is completely unrelated to PSII, the fusion protein restores higher rates of activity upon rebinding to PSII than either the native spinach MSP, or T. elongatus MSP. PSII reconstituted with the fusion protein also has a lower requirement for calcium than PSII with the small extrinsic proteins removed, or PSII reconstituted with spinach or T. elongatus MSP. The MSP portion of the fusion protein is less thermally stable compared to isolated MSP from T. elongatus, which could be the key to its superior activation capability through greater flexibility. This work reveals the importance of protein-protein interactions in the water splitting activity of PSII and suggests that conformational configurations, which increase flexibility in MSP, are essential to its function, even when these are induced by an unrelated protein.

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“…Photosystem II (PSII) contains a set of intrinsic membrane proteins (PsbA, B, C, D, E, and F) that appear to function either directly or indirectly as the ligation sites for the organic and inorganic components of the electron transfer chain (Eaton-Rye and Putnam-Evans 2005; Nixon et al 2005). It also contains a number of small peptides that are involved in assembly and stabilization of the multisubunit complex (Thornton et al 2005).…”

Section: Introductionmentioning

confidence: 99%

The PSII calcium site revisited

2007

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Oxidation of H 2 O by photosystem II is a unique redox reaction in that it requires Ca 2+ as well as Cl -as obligatory activators/cofactors of the reaction, which is catalyzed by Mn atoms. The properties of the binding site for Ca 2+ in this reaction resemble those of other Ca 2+ binding proteins, and recent X-ray structural data confirm that the metal is in fact ligated at least in part by amino acid side chain oxo anions. Removal of Ca 2+ blocks water oxidation chemistry at an early stage in the cycle of redox reactions that result in O-O bond formation, and the intimate involvement of Ca 2+ in this reaction that is implied by this result is confirmed by an ever-improving set of crystal structures of the cyanobacterial enzyme. Here, we revisit the photosystem II Ca 2+ site, in part to discuss the additional information that has appeared since our earlier review of this subject (van Gorkom HJ, Yocum CF In: Wydrzynski TJ, Satoh K (eds) Photosystem II: the light-driven water:plastoquinone oxidoreductase), and also to reexamine earlier data, which lead us to conclude that all S-state transitions require Ca 2+ .

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The D1 and D2 Core Proteins

Cited by 13 publications

References 201 publications

Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms

Structural and functional aspects of the MSP (PsbO) and study of its differences in thermophilic versus mesophilic organisms

The importance of protein–protein interactions for optimising oxygen activity in photosystem II: reconstitution with a recombinant thioredoxin—manganese stabilising protein

The PSII calcium site revisited

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