Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II

Fromme, Petra; Kern, Jan; Loll, Bernhard; Biesiadka, Jaceck; Saenger, Wolfram; Witt, H. T.; Krauß, Norbert; Zouni, Athina

doi:10.1098/rstb.2002.1143

Cited by 47 publications

(42 citation statements)

References 43 publications

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“…Structural analyses of cyanobacterial PSII by X-ray crystallography with atomic resolutions of 2.9-3.5 Å have established the arrangement of the cofactors and pigments (Fig. 2) (Biesiadka et al 2004;Ferreira et al 2004;Fromme et al 2002;Guskov et al 2009a;Kamiya and Shen 2003;Loll et al 2005;Zouni et al 2001), which are all within energy transfer or electron tunneling distance of each other. The functional motif for water oxidation consists of: a chlorophyll a dimer, P D1 P D2 , and the primary electron donor chlorophyll a, Chl D1 (which collectively with Chl D2 is referred to as P680); the primary electron acceptor pheophytin a; Pheo D1 ; the plastoquinone acceptors, Q A , Q B , and Q C ; the redox-active tyrosine, Y Z ; and the tetranuclear manganese/calcium cluster, Mn 4 Ca.…”

Section: Contemporary Photosystem Ii: a Closer Lookmentioning

confidence: 98%

The evolution of Photosystem II: insights into the past and future

et al. 2010

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This article attempts to address the molecular origin of Photosystem II (PSII), the central component in oxygenic photosynthesis. It discusses the possible evolution of the relevant cofactors needed for splitting water into molecular O2 with respect to the following functional domains in PSII: the reaction center (RC), the oxygen evolving complex (OEC), and the manganese stabilizing protein (MSP). Possible ancestral sources of the relevant cofactors are considered, as are scenarios of how these components may have been brought together to produce the intermediate steps in the evolution of PSII. Most importantly, the driving forces that maintained these intermediates for continued adaptation are considered. We then apply our understanding of the evolution of PSII to the bioengineering of a water oxidizing catalyst for utilization of solar energy.

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Section: Contemporary Photosystem Ii: a Closer Lookmentioning

confidence: 98%

The evolution of Photosystem II: insights into the past and future

et al. 2010

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“…Many advances have been made recently in understating the S-cycle, using a combination of structural and spectroscopic methods; however, some details remain a matter of debate. The details and current theories of the molecular mechanism of water oxidation have been reviewed in the following references: (Ahrling et al 2005;Barber 2003;Britt et al 2004;Fromme et al 2002;Haumann et al 2005a, b;Hillier and Wydrzynski 2004;Messinger 2004;Razeghifard et al 2005). The organization of the [Mn 4 Ca] cluster was determined from recent crystal structures (Ferreira et al 2004;Loll et al 2005b) and details of its structure are reviewed in Barber (2006a, b), Biesiadka et al (2004), Kern et al (2007), Yachandra (2005), and Yano et al (2006).…”

Section: Introductionmentioning

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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“…Otherwise, the absence of any electrostatic effect of the D1-E189 mutants could be explained by a distance between Y Z and D1-H190, D1-E189 which is much greater than so far supposed. The advanced crystal structure of PSII (see Fromme et al 2002) indicates that the D1-His-190 may indeed be more than 10 Å away from the position of Y Z .…”

Section: A Special Role Of D1-his190 In the Acid Or Base Cluster Aroumentioning

confidence: 99%

Electrostatics and proton transfer in photosynthetic water oxidation

Junge

Haumann

Ahlbrink

et al. 2002

Phil. Trans. R. Soc. Lond. B

129

131

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Photosystem II (PSII) oxidizes two water molecules to yield dioxygen plus four protons. Dioxygen is released during the last out of four sequential oxidation steps of the catalytic centre (S 0 ⇒ S 1 , S 1 ⇒ S 2 , S 2 ⇒ S 3 , S 3 ⇒ S 4 → S 0 ). The release of the chemically produced protons is blurred by transient, highly variable and electrostatically triggered proton transfer at the periphery (Bohr effect). The extent of the latter transiently amounts to more than one H ϩ /e Ϫ under certain conditions and this is understood in terms of electrostatics. By kinetic analyses of electron-proton transfer and electrochromism, we discriminated between Bohr-effect and chemically produced protons and arrived at a distribution of the latter over the oxidation steps of 1 : 0 : 1 : 2. During the oxidation of tyr-161 on subunit D1 (Y Z ), its phenolic proton is not normally released into the bulk. Instead, it is shared with and confined in a hydrogenbonded cluster. This notion is difficult to reconcile with proposed mechanisms where Y Z acts as a hydrogen acceptor for bound water. Only in manganese (Mn) depleted PSII is the proton released into the bulk and this changes the rate of electron transfer between Y Z and the primary donor of PSII P ϩ 680 from electron to proton controlled. D1-His190, the proposed centre of the hydrogen-bonded cluster around Y Z , is probably further remote from Y Z than previously thought, because substitution of D1-Glu189, its direct neighbour, by Gln, Arg or Lys is without effect on the electron transfer from Y Z to P

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Functional implications on the mechanism of the function of photosystem II including water oxidation based on the structure of photosystem II

Cited by 47 publications

References 43 publications

The evolution of Photosystem II: insights into the past and future

The evolution of Photosystem II: insights into the past and future

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

Electrostatics and proton transfer in photosynthetic water oxidation

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