Photosystem II: The Solid Structural Era

Rhee, Kyong−Hi

doi:10.1146/annurev.biophys.30.1.307

Cited by 39 publications

(19 citation statements)

References 141 publications

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“…An important step towards a more detailed insight into the structure of PS II was the development of a method for growing 2D crystals of monomeric D1/D2/CP47 PS II subcomplexes from spinach by Inoue and coworkers (1996) and 2D and 3D structure analysis of this material. The method was significantly improved and resolutions of 8 -6 Å obtained by cryo-electron-microscopy of this sample type Rhee et al 1997Rhee et al , 1998Rhee 2001). This achievement offered for the first time information on the arrangement of the central subunits as well as of cofactors of the reaction center and the internal antenna system.…”

Section: Overall Structure Of Psiimentioning

confidence: 96%

Photosystem II: Structure and mechanism of the water:plastoquinone oxidoreductase

2007

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This mini-review briefly summarizes our current knowledge on the reaction pattern of light-driven water splitting and the structure of Photosystem II that acts as a water:plastoquinone oxidoreductase. The overall process comprises three types of reaction sequences: (a) light-induced charge separation leading to formation of the radical ion pair P680+*QA(-*) ; (b) reduction of plastoquinone to plastoquinol at the QB site via a two-step reaction sequence with QA(-*) as reductant and (c) oxidative water splitting into O2 and four protons at a manganese-containing catalytic site via a four-step sequence driven by P680+* as oxidant and a redox active tyrosine YZ acting as mediator. Based on recent progress in X-ray diffraction crystallographic structure analysis the array of the cofactors within the protein matrix is discussed in relation to the functional pattern. Special emphasis is paid on the structure of the catalytic sites of PQH2 formation (QB-site) and oxidative water splitting (Mn4OxCa cluster). The energetics and kinetics of the reactions taking place at these sites are presented only in a very concise manner with reference to recent up-to-date reviews. It is illustrated that several questions on the mechanism of oxidative water splitting and the structure of the catalytic sites are far from being satisfactorily answered.

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Section: Overall Structure Of Psiimentioning

confidence: 96%

Photosystem II: Structure and mechanism of the water:plastoquinone oxidoreductase

2007

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“…Significant advances in X-ray crystallography of Photosystem II (PSII) were made over the past decade, starting with the first X-ray crystal model of the PSII protein complex obtained at 3.8 Å resolution [1,2]. Subsequent work resolved the structure of PSII at 3.5 Å resolution and proposed a detailed atomistic model of the oxygen-evolving complex (OEC), responsible for catalytic water oxidation [3].…”

Section: Introductionmentioning

confidence: 99%

Oxomanganese complexes for natural and artificial photosynthesis

Rivalta

Brudvig

Batista

2012

Current Opinion in Chemical Biology

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The oxygen-evolving complex (OEC) of Photosystem II (PSII), is an oxomanganese complex that catalyzes water-splitting into O2, protons and electrons. Recent breakthroughs in X-ray crystallography have resolved the cuboidal OEC structure at 1.9 Å resolution, stimulating significant interest in studies of structure/function relations. This article summarizes recent advances on studies of the OEC along with studies of synthetic oxomanganese complexes for artificial photosynthesis. Quantum mechanics/molecular mechanics hybrid methods have enabled modeling the S1 state of the OEC, including the ligation proposed by the most recent X-ray data where D170 is bridging Ca and the Mn center outside the CaMn3 core. Molecular dynamics and Monte Carlo simulations have explored the structural/functional roles of chloride, suggesting that it regulates the electrostatic interactions between D61 and K317 that might be critical for proton abstraction. Furthermore, structural studies of synthetic oxomanganese complexes, including the [H2O(terpy)MnIII(μ-O)2MnIV(terpy)OH2]3+ (1, terpy=2,2′:6′,2″-terpyridine) complex, provided valuable insights on the mechanistic influence of carboxylate moieties in close contact with the Mn catalyst during oxygen evolution. Covalent attachment of 1 to TiO2 has been achieved via direct deposition and by using organic chromophoric linkers. The (III,IV) oxidation state of 1 attached to TiO2 can be advanced to (IV,IV) by visible-light photoexcitation, leading to photoinduced interfacial electron transfer. These studies are particularly relevant to the development of artificial photosynthetic devices based on inexpensive materials.

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“…Single particle analysis on PSII preparations from different species (plants, algae, cyanobacteria) gave insights in organization, size, subunit composition of supercomplexes (containing various external antenna proteins) as well as of PSII core (without external antenna proteins) or subcore complexes (missing some of the integral proteins) (see for example Rögner et al 1987;Haag et al 1990;Holzenburg et al 1993;Santini et al 1994;Boekema et al 1995;Tsiotis et al 1996;Barber et al 1999;Boekema et al 2000;Nield et al 2000;Yakushevska et al 2003). A further important step towards a more detailed insight into the structure of PSII was achieved by 2D crystallization (Nakazato et al 1996) and the elucidation of a 2D and later a 3D structural model of monomeric D1/D2/CP47 PSII subcomplex from spinach at a resolution of 8-6 Å by cryo-electron-microscopy Rhee et al 1997Rhee et al , 1998Rhee 2001). For the first time the arrangement of the central subunits as well as of cofactors and the internal antenna system could be identified.…”

Section: Introductionmentioning

confidence: 99%

Structure of the Mn4–Ca cluster as derived from X-ray diffraction

et al. 2007

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The catalytic centre for light-induced water oxidation in photosystem II (PSII) is a multinuclear metal cluster containing four manganese and one calcium cations. Knowing the structure of this biological catalyst is of utmost importance for unravelling the mechanism of water oxidation in photosynthesis. In this review we describe the current state of the X-ray structure determination at 3.0 A resolution of the water oxidation complex (WOC) of PSII. The arrangement of metal cations in the cluster, their coordination and protein surroundings are discussed with regard to spectroscopic and mutagenesis studies. Limitations of the presently available structural data are pointed out and possible perspectives for the future are outlined, including the combination of X-ray diffraction and X-ray spectroscopy on single crystals.

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Photosystem II: The Solid Structural Era

Cited by 39 publications

References 141 publications

Photosystem II: Structure and mechanism of the water:plastoquinone oxidoreductase

Photosystem II: Structure and mechanism of the water:plastoquinone oxidoreductase

Oxomanganese complexes for natural and artificial photosynthesis

Structure of the Mn4–Ca cluster as derived from X-ray diffraction

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