Introduction to the Photosystem II Reaction Center– Isolation and Biochemical and Biophysical Characterization

Satoh, Kimiyuki

doi:10.1007/0-306-48127-8_11

Cited by 18 publications

(8 citation statements)

References 102 publications

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“…These included the core proteins, D1 and D2 for PSII and PsaA and PsaB for PSI, which are generally accepted as being essential (Nechushtai et al, 1996;Satoh, 1996). Chl-binding proteins (CP-43 and CP-47) are also typically found associated with the PSII complex (Bricker and Ghanotakis, 1996), as well as cyt b 559 (Whitmarsh and Pakrasi, 1996).…”

Section: Discussionmentioning

confidence: 99%

Mollusc-Algal Chloroplast Endosymbiosis. Photosynthesis, Thylakoid Protein Maintenance, and Chloroplast Gene Expression Continue for Many Months in the Absence of the Algal Nucleus

et al. 2000

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Early in its life cycle, the marine mollusc Elysia chlorotica Gould forms an intracellular endosymbiotic association with chloroplasts of the chromophytic alga Vaucheria litorea C. Agardh. As a result, the dark green sea slug can be sustained in culture solely by photoautotrophic CO 2 fixation for at least 9 months if provided with only light and a source of CO 2 . Here we demonstrate that the sea slug symbiont chloroplasts maintain photosynthetic oxygen evolution and electron transport activity through photosystems I and II for several months in the absence of any external algal food supply. This activity is correlated to the maintenance of functional levels of chloroplast-encoded photosystem proteins, due in part at least to de novo protein synthesis of chloroplast proteins in the sea slug. Levels of at least one putative algal nuclear encoded protein, a light-harvesting complex protein homolog, were also maintained throughout the 9-month culture period. The chloroplast genome of V. litorea was found to be 119.1 kb, similar to that of other chromophytic algae. Southern analysis and polymerase chain reaction did not detect an algal nuclear genome in the slug, in agreement with earlier microscopic observations. Therefore, the maintenance of photosynthetic activity in the captured chloroplasts is regulated solely by the algal chloroplast and animal nuclear genomes.

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Section: Discussionmentioning

confidence: 99%

Mollusc-Algal Chloroplast Endosymbiosis. Photosynthesis, Thylakoid Protein Maintenance, and Chloroplast Gene Expression Continue for Many Months in the Absence of the Algal Nucleus

et al. 2000

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“…However, D1-Glu130 of spinach seems to be protonated due to a stronger hydrogen bond relative to Synechocystis. The calculated pI of the D1 protein was 5.45 in Synechocystis and 5.10 in spinach, and the experimental value of pI was 5.2 in PS II RC in spinach (Satoh 1996). One of the reasons for pheophytinization may be the acidity of the Pheo a environment.…”

Section: Assignments Of Pheo a Moleculesmentioning

confidence: 99%

Isolation and spectral characterization of Photosystem II reaction center from Synechocystis sp. PCC 6803

et al. 2008

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We isolated highly-purified photochemically active photosystem (PS) II reaction center (RC) complexes from the cyanobacterium Synechocystis sp. PCC 6803 using a histidine-tag introduced to the 47 kDa chlorophyll protein, and characterized their spectroscopic properties. Purification was carried out in a one-step procedure after isolation of PS II core complex. The RC complexes consist of five polypeptides, the same as in spinach. The pigment contents per two molecules of pheophytin a were 5.8 +/- 0.3 chlorophyll (Chl) a and 1.8 +/- 0.1 beta-carotene; one cytochrome b(559) was found per 6.0 Chl a molecules. Overall absorption and fluorescence properties were very similar to those of spinach PS II RCs; our preparation retains the best properties so far isolated from cyanobacteria. However, a clear band-shift of pheophytin a and beta-carotene was observed. Reasons for these differences, and RC composition, are discussed on the basis of the three-dimensional structure of complexes.

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“…The ultrastructure of thylakoid membranes of barley (55, SO), spinach (85,119,120,122), maize (84), lettuce (56), soybean (67), Alocasia (7), and pea (11,101) have all been analyzed by freeze-etch and freeze-fracture electron microscopy and show marked similarities (see 80,121). The protein complexes detected in these analyses were named according to the surfaces with which they were associated (e.g.…”

Section: Arrangement Of Psii In the Thylakoid Membranementioning

confidence: 99%

Structure and Membrane Organization of Photosystem Ii in Green Plants

Hankamer

Barber

Boekema

1997

Annu. Rev. Plant. Physiol. Plant. Mol. Biol.

337

216

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Photosystem II (PSII) is the pigment protein complex embedded in the thylakoid membrane of higher plants, algae, and cyanobacteria that uses solar energy to drive the photosynthetic water-splitting reaction. This chapter reviews the primary, secondary, tertiary, and quaternary structures of PSII as well as the function of its constituent subunits. The understanding of in vivo organization of PSII is based in part on freeze-etched and freeze-fracture images of thylakoid membranes. These images show a resolution of about 40-50 A and so provide information mainly on the localization, heterogeneity, dimensions, and shapes of membrane-embedded PSII complexes. Higher resolution of about 15-40 A has been obtained from single particle images of isolated PSII complexes of defined and differing subunit composition and from electron crystallography of 2-D crystals. Observations are discussed in terms of the oligomeric state and subunit organization of PSII and its antenna components.

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Introduction to the Photosystem II Reaction Center– Isolation and Biochemical and Biophysical Characterization

Cited by 18 publications

References 102 publications

Mollusc-Algal Chloroplast Endosymbiosis. Photosynthesis, Thylakoid Protein Maintenance, and Chloroplast Gene Expression Continue for Many Months in the Absence of the Algal Nucleus

Mollusc-Algal Chloroplast Endosymbiosis. Photosynthesis, Thylakoid Protein Maintenance, and Chloroplast Gene Expression Continue for Many Months in the Absence of the Algal Nucleus

Isolation and spectral characterization of Photosystem II reaction center from Synechocystis sp. PCC 6803

Structure and Membrane Organization of Photosystem Ii in Green Plants

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