Isolation of a photosystem 2 preparation from higher plants with highly enriched oxygen evolution activity

Ford, Robert C.; Evans, M.C.W.

doi:10.1016/0014-5793(83)80957-0

Cited by 299 publications

(143 citation statements)

References 17 publications

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“…PSII membranes were isolated from fresh spinach leaves (Spinacia oleracea) purchased from a local market, by using the method of Berthold et al (41)(42)(43). Before PSII isolation, spinach leaves were kept in darkness to allow for dark adaptation.…”

Section: Methodsmentioning

confidence: 99%

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Kale

Hebert

Frankel

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

134

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The Photosystem II reaction center is vulnerable to photoinhibition. The D1 and D2 proteins, lying at the core of the photosystem, are susceptible to oxidative modification by reactive oxygen species that are formed by the photosystem during illumination. Using spin probes and EPR spectroscopy, we have determined that both O 2 . The identification of specific amino acid residues oxidized by reactive oxygen species provides insights into the mechanism of damage to the D1 and D2 proteins under light stress.photosynthesis | Photosystem II | reactive oxygen species | photo inhibition | mass spectrometry P hotosystem II (PSII) functions as a water-plastoquinone oxidoreductase (1, 2) and is a thylakoid membrane pigmentprotein complex present in all oxygenic photosynthetic organisms (cyanobacteria, algae, and higher plants). Current high-resolution structures of thermophilic cyanobacterial PSII (3, 4), and lower resolution structures of the red algal (5) and higher plant photosystems (6), have been critically important in furthering our understanding of the molecular organization of PSII. Structurally, the PSII reaction center core is composed of five proteins: D1, D2, the α-and β-subunits of cytochrome b 559 , and PsbI. These components bind all of the redox-active cofactors of PSII.Excitation energy transfer and electron transport within PSII are unavoidably associated with production of reactive oxygen species (ROS) when the absorption of light by the chlorophyll antenna exceeds the capacity for energy utilization. Many mechanisms for ROS production have been proposed (for reviews, see refs. 7 and 8). Briefly, singlet oxygen ( 1 O 2 ) may be formed by excitation energy transfer from triplet chlorophylls (formed either by the change in orientation of the spin of an excited electron in the PSII antenna complex, or via charge recombination of the primary radical pair 3 [P 680 •+ Pheo •− ]) to O 2 (9, 10). ROS production by electron transport involves either the two-electron oxidation of water or the one-electron reduction of O 2 on the PSII electron donor and acceptor sides, respectively. On the PSII electron donor side, a twoelectron oxidation of water leads to the formation of hydrogen peroxide (H 2 O 2 ), which may be oxidized to the superoxide anion radical (O 2•−

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Section: Methodsmentioning

confidence: 99%

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Kale

Hebert

Frankel

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

134

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“…Oxygen evolving photosystem II subchloroplast membranes were prepared from market spinach by the method of Ford and Evans [11]. Samples were prepared as in [8] except that 0.5 mM p-phenyl benzoquinone replaced di-methyl benzoquinone and 1% methanol, either per-deuterated or protonated, was added.…”

Section: Methodsmentioning

confidence: 99%

Investigation of the interaction of the water oxidising manganese complex of photosystem II with the aqueous solvent environment

1999

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Interaction of the water oxidising manganese complex of photosystem II with the aqueous environment has been investigated using electron paramagnetic resonance spectroscopy and electron spin echo envelope modulation spectroscopy to detect interaction of [ 2 H]methanol with the complex in the S 2 state. The experiments show that the classical S 2 multiline signal is associated with a manganese environment which is not exposed to the aqueous medium. An electron paramagnetic resonance spectroscopy signal, also induced by 200 K illumination, showing 2 H modulation by methanol in the medium and a modified multiline electron paramagnetic resonance spectroscopy signal formed in parallel to it, are suggested to be associated with a second manganese environment exposed to the medium.z 1999 Federation of European Biochemical Societies.

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“…PS II preparations with 150 Chl/cyt b559 were isolated by the method of Ford and Evans [19] from market spinach (Spinacea oleracea).…”

Section: Methodsmentioning

confidence: 99%

Electron transfer in the isolated photosystem II reaction centre complex

Nugent¹,

Telfer²,

Demetriou³

et al. 1989

FEBS Letters

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We have characterised the electron-transfer properties of the D 1/D2/cytochrome b-559 complex using EPR spectrometry. The complex can transfer electrons to silicomolybdate and ferricyanide at cryogenic temperatures. In the presence of silicomolybdate or ferricyanide, two chlorophyll cation radicals were observed from P680 ÷ (0.8 mT) and monomeric Chl (1.0 mT). Reduction of silicomolybdate was detected as a 2.7 mT signal at g = 1.942. A radical attributed to a tyrosine cation radical (D ÷/Z ÷) was also observed in a small percentage of centres.

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Isolation of a photosystem 2 preparation from higher plants with highly enriched oxygen evolution activity

Cited by 299 publications

References 17 publications

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II

Investigation of the interaction of the water oxidising manganese complex of photosystem II with the aqueous solvent environment

Electron transfer in the isolated photosystem II reaction centre complex

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