Release of polypeptides from highly active O<sub>2</sub>‐evolving photosystem‐2 preparation by this treatment

Yamamoto, Yasusi; Doi, Mitsunobu; Tamura, Noriaki; Nishimura, Mitsuo

doi:10.1016/0014-5793(81)80520-0

Cited by 247 publications

(87 citation statements)

References 20 publications

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“…At increased Tris concentration, the same polypeptide was present in the supernatant albeit in increased amounts (Figure 4 A and Figure 5). The loss of a polypeptide of similar size has earlier been reported (29,34). In contrast, the same treatments performed at pH 6.5 or treatments with Hepes buffer at pH 8.5 were unable to remove any polypeptides from the vesicles (Figure 4 A).…”

Section: Effect Of Tris Washing On the Polypeptide Composition Of Inssupporting

confidence: 81%

Reactivation of photosynthetic oxygen evolution in tris-inactivated inside-out photosystem II vesicles from spinach

Henry

Møller

Andersson

et al. 1982

Carlsberg Res. Commun.

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Purified inside-out photosystem II vesicles with retained capacity for oxygen evolution and a simple polypeptide composition were found to be more sensitive to washing with tris(hydroxymethyl)aminomethane (Tris) at alkaline pH than right-side out thylakoids. This suggests that the thylakoid membrane limits the penetration of the active unprotonated form of Tris.The inhibition of photosynthetic oxygen evolution by alkaline Tris-washing (pH 8.5) coincided with the release of a polypeptide with a molecular weight of 32,000 from the inside-out vesicles. Only this polypeptide was released with concentrations of Tris up to 200 mM, while higher concentrations removed additional polypeptides with a molecular weight of 34,000 and 56,000. About 70 96 of the membrane bound manganese is lost by washing the vesicles with 200 mM-Tris. Oxygen evolution was not inhibited nor were polypeptides released with Tris buffered at pH 6.5. From right-side out thylakoids the 32,000 molecular weight polypeptide could not be extracted into the ambient medium by Tris-washing.Restoration of oxygen evolution of Tris-inactivated inside-out and right-side out vesicles was possible with the aid of reduced dichlorophenol indophenol but without the addition of the 32,000 molecular weight polypeptide or manganese.Abbreviations: Chl = chlorophyll; DCMU = 3-(3,4-dichlorophenyl)-l,l-dimethyl urea; DCPIP = 2,6-dichlorophenol indophenol; Hepes = N-2-hydroxyethylpiperazine-N'-2-ethane sulfonic acid; TMBZ = tetramethylbenzidine; Tris = tris(hydroxymethyl)aminomethane.

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Section: Effect Of Tris Washing On the Polypeptide Composition Of Inssupporting

confidence: 81%

Reactivation of photosynthetic oxygen evolution in tris-inactivated inside-out photosystem II vesicles from spinach

Henry

Møller

Andersson

et al. 1982

Carlsberg Res. Commun.

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“…2, blue trace). In this sample, the OEC is inactivated with 1.8 M alkaline Tris (24), Y Z is the terminal electron donor (25,26), and reaction 5 in Fig. 1 A is blocked.…”

Section: Resultsmentioning

confidence: 99%

Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle

Barry

Cooper²,

Riso³

et al. 2006

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

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Photosynthetic oxygen production by photosystem II (PSII) is responsible for the maintenance of aerobic life on earth. The production of oxygen occurs at the PSII oxygen-evolving complex (OEC), which contains a tetranuclear manganese (Mn) cluster. Photo-induced electron transfer events in the reaction center lead to the accumulation of oxidizing equivalents on the OEC. Four sequential photooxidation reactions are required for oxygen production. The oxidizing complex cycles among five oxidation states, called the S n states, where n refers to the number of oxidizing equivalents stored. Oxygen release occurs during the S 3-to-S0 transition from an unstable intermediate, known as the S4 state. In this report, we present data providing evidence for the production of an intermediate during each S state transition. These proteinderived intermediates are produced on the microsecond to millisecond time scale and are detected by time-resolved vibrational spectroscopy on the microsecond time scale. Our results suggest that a protein-derived conformational change or proton transfer reaction precedes Mn redox reactions during the S 2-to-S3 and S 3-to-S0 transitions.manganese cluster ͉ photosynthesis ͉ photosystem II ͉ time-resolved IR ͉ water oxidation T ime-resolved vibrational spectroscopy can detect chemical intermediates formed during enzymatic catalysis. Advantages include the technique's exquisite structural sensitivity and its high temporal resolution. Recent advances in methodology and interpretation have produced insights into the catalytic mechanism in several biological systems (for examples, see refs. 1-4).In this paper, we report the use of time-resolved IR spectroscopy to investigate the mechanism of photosynthetic water oxidation. Photosystem II (PSII) catalyzes the oxidation of water and the reduction of bound plastoquinone. Photoexcitation of PSII leads to the oxidation of the chlorophyll donor, P 680 , and the sequential reduction of a pheophytin (Fig. 1A, reaction 1) and a plastoquinone, Q A ( Fig. 1 A, reaction 2), in picoseconds. Q A reduces Q B to generate a semiquinone radical, Q B Ϫ , on the microsecond time scale (Fig. 1 A, reaction 3 ) (reviewed in ref. 5).A second photoexcitation leads to the reduction and protonation of Q B Ϫ to form the quinol Q B H 2 . The rate of reduction of Q B is faster than the rate of reduction of Q B Ϫ (see ref. 6 and references therein), which gives rise to a characteristic period-2 oscillation in kinetics originating on the PSII acceptor side (7).The primary chlorophyll donor, P 680 , oxidizes a tyrosine, Y Z (Y161 in the D1 subunit), on the nanosecond to microsecond time scale (Fig. 1 A, reaction 4). In turn, tyrosine Y Z ⅐ oxidizes the oxygen-evolving complex (OEC) on every flash (Fig. 1 A, reaction 5) (8). Four sequential photooxidation reactions are required for oxygen production, and the oxidizing complex cycles among five oxidation states, called the S n states, where n refers to the number of oxidizing equivalents stored (9). The rate of OEC oxidation slows as o...

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“…Purification Procedures of Five Extrinsic Proteins-The crude PSII suspended in 10 mM MES-NaOH (pH 6.5) (buffer C) was treated with 1 M Tris-HCl (pH 8.5) at 0.5 mg of Chl/ml for 1 h on ice in the dark to release all of the extrinsic proteins of PsbO, PsbQЈ, PsbV, Psb31, and PsbU (29,30,33). The treated samples were centrifuged at 227,000 ϫ g for 30 min after addition of 14% PEG 1450.…”

Section: Methodsmentioning

confidence: 99%

“…In spinach PSII, the PsbP and PsbQ proteins are selectively released with 1 M NaCl-wash (37), and all of the three extrinsic proteins of PsbO, PsbP, and PsbQ can be released with 1 M CaCl 2 (38), 2.6 M urea plus 0.2 M NaCl (39), or 1 M Tris (pH 8.5) treatment (33). In red algal PSII, no extrinsic proteins are released by 1 M NaCl wash, whereas treatments with 1 M CaCl 2 , 2.6 M urea plus 0.2 M NaCl, or 1 M Tris (pH 8.5) released all of the extrinsic proteins (4,5).…”

Section: Dissociation Of Extrinsic Proteins By Various Treatments-mentioning

confidence: 99%

Binding and Functional Properties of Five Extrinsic Proteins in Oxygen-evolving Photosystem II from a Marine Centric Diatom, Chaetoceros gracilis*

Nagao

Moriguchi

Tomo

et al. 2010

Journal of Biological Chemistry

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Oxygen-evolving photosystem II (PSII) isolated from a marine centric diatom, Chaetoceros gracilis, contains a novel extrinsic protein (Psb31) in addition to four red algal type extrinsic proteins of PsbO, PsbQ , PsbV, and PsbU. In this study, the five extrinsic proteins were purified from alkaline Tris extracts of the diatom PSII by anion and cation exchange chromatographic columns at different pH values. Reconstitution experiments in various combinations with the purified extrinsic proteins showed that PsbO, PsbQ , and Psb31 rebound directly to PSII in the absence of other extrinsic proteins, indicating that these extrinsic proteins have their own binding sites in PSII intrinsic proteins. On the other hand, PsbV and PsbU scarcely rebound to PSII alone, and their effective bindings required the presence of all of the other extrinsic proteins. Interestingly, PSII reconstituted with Psb31 alone considerably restored the oxygen evolving activity in the absence of PsbO, indicating that Psb31 serves as a substitute in part for PsbO in supporting oxygen evolution. A significant difference found between PSIIs reconstituted with Psb31 and with PsbO is that the oxygen evolving activity of the former is scarcely stimulated by Cl ؊ and Ca 2؉ ions but that of the latter is largely stimulated by these ions, although rebinding of PsbV and PsbU activated oxygen evolution in the absence of Cl ؊ and Ca 2؉ ions in both the former and latter PSIIs. Based on these results, we proposed a model for the association of the five extrinsic proteins with intrinsic proteins in diatom PSII and compared it with those in PSIIs from the other organisms.

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Release of polypeptides from highly active O₂‐evolving photosystem‐2 preparation by this treatment

Cited by 247 publications

References 20 publications

Reactivation of photosynthetic oxygen evolution in tris-inactivated inside-out photosystem II vesicles from spinach

Reactivation of photosynthetic oxygen evolution in tris-inactivated inside-out photosystem II vesicles from spinach

Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle

Binding and Functional Properties of Five Extrinsic Proteins in Oxygen-evolving Photosystem II from a Marine Centric Diatom, Chaetoceros gracilis*

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Release of polypeptides from highly active O2‐evolving photosystem‐2 preparation by this treatment

Cited by 247 publications

References 20 publications

Reactivation of photosynthetic oxygen evolution in tris-inactivated inside-out photosystem II vesicles from spinach

Reactivation of photosynthetic oxygen evolution in tris-inactivated inside-out photosystem II vesicles from spinach

Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle

Binding and Functional Properties of Five Extrinsic Proteins in Oxygen-evolving Photosystem II from a Marine Centric Diatom, Chaetoceros gracilis*

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Release of polypeptides from highly active O₂‐evolving photosystem‐2 preparation by this treatment