Electrochemically produced hydrogen peroxide affects Joliot-type oxygen-evolution measurements of photosystem II
The main technique employed to characterize the efficiency of water-splitting in photosynthetic preparations in terms of miss and double hit parameters and for the determination of Si (i=2,3,0) state lifetimes is the measurement of flash-induced oxygen oscillation pattern on bare platinum (Joliot-ty...
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| Published in | Biochimica et biophysica acta Vol. 1837; no. 9; pp. 1411 - 1416 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
01.09.2014
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| Abstract | The main technique employed to characterize the efficiency of water-splitting in photosynthetic preparations in terms of miss and double hit parameters and for the determination of Si (i=2,3,0) state lifetimes is the measurement of flash-induced oxygen oscillation pattern on bare platinum (Joliot-type) electrodes. We demonstrate here that this technique is not innocent. Polarization of the electrode against an Ag/AgCl electrode leads to a time-dependent formation of hydrogen peroxide by two-electron reduction of dissolved oxygen continuously supplied by the flow buffer. While the miss and double hit parameters are almost unaffected by H₂O₂, a time dependent reduction of S1 to S₋₁ occurs over a time period of 20 min. The S1 reduction can be largely prevented by adding catalase or by removing O₂ from the flow buffer with N₂. Importantly, we demonstrate that even at the shortest possible polarization times (40s in our set up) the S₂ and S₀ decays are significantly accelerated by the side reaction with H₂O₂. The removal of hydrogen peroxide leads to unperturbed S₂ state data that reveal three instead of the traditionally reported two phases of decay. In addition, even under the best conditions (catalase+N₂; 40s polarization) about 4% of S₋₁ state is observed in well dark-adapted samples, likely indicating limitations of the equal fit approach. This article is part of a special issue entitled: photosynthesis research for sustainability: keys to produce clean energy. |
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| AbstractList | The main technique employed to characterize the efficiency of water-splitting in photosynthetic preparations in terms of miss and double hit parameters and for the determination of S-i (i = 2,3,0) state lifetimes is the measurement of flash-induced oxygen oscillation pattern on bare platinum (Joliot-type) electrodes. We demonstrate here that this technique is not innocent. Polarization of the electrode against an Ag/AgCl electrode leads to a time-dependent formation of hydrogen peroxide by two-electron reduction of dissolved oxygen continuously supplied by the flow buffer. While the miss and double hit parameters are almost unaffected by H2O2, a time dependent reduction of S-1 to S-1 occurs over a time period of 20 mm. The S-1 reduction can be largely prevented by adding catalase or by removing O-2 from the flow buffer with N-2. Importantly, we demonstrate that even at the shortest possible polarization times (40 s in our set up) the S-2 and S-0 decays are significantly accelerated by the side reaction with H2O2. The removal of hydrogen peroxide leads to unperturbed S-2 state data that reveal three instead of the traditionally reported two phases of decay. In addition, even under the best conditions (catalase + N-2; 40 s polarization) about 4% of S-1 state is observed in well dark-adapted samples, likely indicating limitations of the equal fit approach. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: Keys to Produce Clean Energy. (C) 2014 Elsevier B.V. All rights reserved. The main technique employed to characterize the efficiency of water-splitting in photosynthetic preparations in terms of miss and double hit parameters and for the determination of S-i (i = 2,3,0) state lifetimes is the measurement of flash-induced oxygen oscillation pattern on bare platinum (Joliot-type) electrodes. We demonstrate here that this technique is not innocent. Polarization of the electrode against an Ag/AgCl electrode leads to a time-dependent formation of hydrogen peroxide by two-electron reduction of dissolved oxygen continuously supplied by the flow buffer. While the miss and double hit parameters are almost unaffected by H2O2, a time dependent reduction of S-1 to S-1 occurs over a time period of 20 mm. The S-1 reduction can be largely prevented by adding catalase or by removing O-2 from the flow buffer with N-2. Importantly, we demonstrate that even at the shortest possible polarization times (40 s in our set up) the S-2 and S-0 decays are significantly accelerated by the side reaction with H2O2. The removal of hydrogen peroxide leads to unperturbed S-2 state data that reveal three instead of the traditionally reported two phases of decay. In addition, even under the best conditions (catalase + N-2; 40 s polarization) about 4% of S-1 state is observed in well dark-adapted samples, likely indicating limitations of the equal fit approach. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: Keys to Produce Clean Energy. The main technique employed to characterize the efficiency of water-splitting in photosynthetic preparations in terms of miss and double hit parameters and for the determination of Si (i=2,3,0) state lifetimes is the measurement of flash-induced oxygen oscillation pattern on bare platinum (Joliot-type) electrodes. We demonstrate here that this technique is not innocent. Polarization of the electrode against an Ag/AgCl electrode leads to a time-dependent formation of hydrogen peroxide by two-electron reduction of dissolved oxygen continuously supplied by the flow buffer. While the miss and double hit parameters are almost unaffected by H₂O₂, a time dependent reduction of S1 to S₋₁ occurs over a time period of 20 min. The S1 reduction can be largely prevented by adding catalase or by removing O₂ from the flow buffer with N₂. Importantly, we demonstrate that even at the shortest possible polarization times (40s in our set up) the S₂ and S₀ decays are significantly accelerated by the side reaction with H₂O₂. The removal of hydrogen peroxide leads to unperturbed S₂ state data that reveal three instead of the traditionally reported two phases of decay. In addition, even under the best conditions (catalase+N₂; 40s polarization) about 4% of S₋₁ state is observed in well dark-adapted samples, likely indicating limitations of the equal fit approach. This article is part of a special issue entitled: photosynthesis research for sustainability: keys to produce clean energy. |
| Author | Messinger, Johannes Pham, Long Vo |
| Author_xml | – sequence: 1 givenname: Long Vo surname: Pham fullname: Pham, Long Vo organization: Department of Chemistry, Chemistry Biology Center (KBC), Umeå University, Linnaeus väg 6, SE-901 87 Umeå, Sweden – sequence: 2 givenname: Johannes surname: Messinger fullname: Messinger, Johannes email: Johannes.Messinger@umu.se organization: Department of Chemistry, Chemistry Biology Center (KBC), Umeå University, Linnaeus väg 6, SE-901 87 Umeå, Sweden. Electronic address: Johannes.Messinger@umu.se |
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| Cites_doi | 10.1039/b808792j 10.1021/bi00397a019 10.1007/BF00046769 10.1016/j.bbabio.2013.01.013 10.1007/978-94-009-0511-5_209 10.1039/b406437b 10.1021/bi300708a 10.1023/A:1016128632704 10.1021/ac901291v 10.1016/S0167-4838(96)00130-6 10.1021/ja076130q 10.1016/j.ccr.2007.09.001 10.1021/bi00454a024 10.1016/0005-2728(78)90043-9 10.1007/s11120-007-9200-2 10.1021/bi00087a017 10.1007/s11120-009-9434-2 10.1021/bi962653r 10.1016/j.bbabio.2012.10.006 10.1073/pnas.1206266109 10.1016/0005-2728(88)90240-X 10.1016/0076-6879(72)24062-9 10.1016/j.bpj.2009.03.007 10.1021/cr950052k 10.1016/S0021-9258(19)50881-X 10.1111/j.1751-1097.1970.tb06017.x 10.1021/j100883a515 10.1021/bi00383a014 10.1016/S0076-6879(84)05016-3 10.1023/A:1020470224740 10.1002/cctc.201000126 10.1039/c2cp40616k 10.1016/0003-2697(77)90428-6 10.1016/0006-291X(65)90401-8 10.1016/0005-2728(86)90211-2 10.1016/S0005-2728(89)80397-4 10.1021/bi9711285 10.1126/science.11536492 10.1074/jbc.M112.342543 10.1016/0014-5793(90)80829-8 10.1016/0003-2697(76)90527-3 10.1126/science.1071184 10.1016/0005-2728(68)90190-4 10.1039/B604389E 10.1021/bi801580e 10.1146/annurev.arplant.53.100301.135212 10.1021/bi034744b 10.1021/bi00245a027 10.1016/0005-2728(87)90077-6 |
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| Keywords | Photosystem II (PSII) Hydrogen peroxide (HO) Oxygen evolving complex (OEC) Water oxidation Manganese |
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| References | Schröder (10.1016/j.bbabio.2014.01.013_bb0175) 1986; 848 Cox (10.1016/j.bbabio.2014.01.013_bb0105) 2013; 1827 Joliot (10.1016/j.bbabio.2014.01.013_bb0050) 1968; 153 Shevela (10.1016/j.bbabio.2014.01.013_bb0240) 2007; 94 Messinger (10.1016/j.bbabio.2014.01.013_bb0145) 1997; 36 Dau (10.1016/j.bbabio.2014.01.013_bb0070) 2008; 252 Messinger (10.1016/j.bbabio.2014.01.013_bb0255) 1991; 30 Buick (10.1016/j.bbabio.2014.01.013_bb0010) 1992; 255 Hillier (10.1016/j.bbabio.2014.01.013_bb0185) 1993; 38 Velthuys (10.1016/j.bbabio.2014.01.013_bb0150) 1978; 502 Kok (10.1016/j.bbabio.2014.01.013_bb0060) 1970; 11 Bouges (10.1016/j.bbabio.2014.01.013_bb0125) 1971; 936 Bradford (10.1016/j.bbabio.2014.01.013_bb0215) 1976; 72 Kok (10.1016/j.bbabio.2014.01.013_bb0135) 1977 Porra (10.1016/j.bbabio.2014.01.013_bb0200) 2002; 73 Antal (10.1016/j.bbabio.2014.01.013_bb0260) 2009; 96 Klauss (10.1016/j.bbabio.2014.01.013_bb0075) 2012; 109 Suzuki (10.1016/j.bbabio.2014.01.013_bb0080) 2008; 47 Sedmak (10.1016/j.bbabio.2014.01.013_bb0220) 1977; 79 Guiles (10.1016/j.bbabio.2014.01.013_bb0140) 1990; 29 Messinger (10.1016/j.bbabio.2014.01.013_bb0195) 1993; 32 Wydrzynski (10.1016/j.bbabio.2014.01.013_bb0180) 1989; 973 Suzuki (10.1016/j.bbabio.2014.01.013_bb0100) 2012; 51 Winget (10.1016/j.bbabio.2014.01.013_bb0190) 1965; 21 Sanchez-Sanchez (10.1016/j.bbabio.2014.01.013_bb0120) 2009; 81 Damjanov (10.1016/j.bbabio.2014.01.013_bb0110) 1966; 70 Kasting (10.1016/j.bbabio.2014.01.013_bb0005) 2002; 296 Katsounaros (10.1016/j.bbabio.2014.01.013_bb0115) 2012; 14 Lardinois (10.1016/j.bbabio.2014.01.013_bb0210) 1996; 1298 Dau (10.1016/j.bbabio.2014.01.013_bb0040) 2010; 2 Siegbahn (10.1016/j.bbabio.2014.01.013_bb0030) 2013; 1827 Beers (10.1016/j.bbabio.2014.01.013_bb0230) 1952; 195 Renger (10.1016/j.bbabio.2014.01.013_bb0055) 2009; 102 Messinger (10.1016/j.bbabio.2014.01.013_bb0205) 1990; 277 Xiong (10.1016/j.bbabio.2014.01.013_bb0015) 2002; 53 Schröder (10.1016/j.bbabio.2014.01.013_bb0170) 1990; 1–4 Yachandra (10.1016/j.bbabio.2014.01.013_bb0020) 1996; 96 Frasch (10.1016/j.bbabio.2014.01.013_bb0155) 1987; 26 Messinger (10.1016/j.bbabio.2014.01.013_bb0250) 1997; 36 de Wijn (10.1016/j.bbabio.2014.01.013_bb0085) 2002; 72 Aebi (10.1016/j.bbabio.2014.01.013_bb0225) 1984; 105 Joliot (10.1016/j.bbabio.2014.01.013_bb0235) 1972; 24 Isgandarova (10.1016/j.bbabio.2014.01.013_bb0095) 2003; 42 Sivaraja (10.1016/j.bbabio.2014.01.013_bb0130) 1988; 936 Lubitz (10.1016/j.bbabio.2014.01.013_bb0045) 2008; 1 Messinger (10.1016/j.bbabio.2014.01.013_bb0065) 2008 Shevela (10.1016/j.bbabio.2014.01.013_bb0245) 2006; 8 Han (10.1016/j.bbabio.2014.01.013_bb0090) 2012; 287 Frasch (10.1016/j.bbabio.2014.01.013_bb0160) 1987; 891 Mano (10.1016/j.bbabio.2014.01.013_bb0165) 1987; 26 Messinger (10.1016/j.bbabio.2014.01.013_bb0025) 2004; 6 Sproviero (10.1016/j.bbabio.2014.01.013_bb0035) 2008; 130 |
| References_xml | – volume: 1 start-page: 15 year: 2008 ident: 10.1016/j.bbabio.2014.01.013_bb0045 article-title: Solar water-splitting into H2 and O2: design principles of photosystem II and hydrogenases publication-title: Energy Environ. Sci. doi: 10.1039/b808792j contributor: fullname: Lubitz – volume: 26 start-page: 7321 year: 1987 ident: 10.1016/j.bbabio.2014.01.013_bb0155 article-title: Kinetics of O2 evolution from H2O2 catalyzed by the oxygen-evolving complex: investigation of the S1-dependent reaction publication-title: Biochemistry doi: 10.1021/bi00397a019 contributor: fullname: Frasch – volume: 38 start-page: 417 year: 1993 ident: 10.1016/j.bbabio.2014.01.013_bb0185 article-title: Increases in Peroxide formation by the photosystem II oxygen-evolving reactions upon removal of the extrinsic 16, 22 and 33kDa proteins are reversed by CaCl2 addition publication-title: Photosynth. Res. doi: 10.1007/BF00046769 contributor: fullname: Hillier – start-page: 291 year: 2008 ident: 10.1016/j.bbabio.2014.01.013_bb0065 article-title: Photosynthetic water-splitting contributor: fullname: Messinger – volume: 1827 start-page: 1020 year: 2013 ident: 10.1016/j.bbabio.2014.01.013_bb0105 article-title: Reflections on substrate water and dioxygen formation publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbabio.2013.01.013 contributor: fullname: Cox – volume: 1–4 start-page: A901 year: 1990 ident: 10.1016/j.bbabio.2014.01.013_bb0170 article-title: Hydrogen-peroxide production in photosystem II preparations publication-title: Curr. Res. Photosynth. doi: 10.1007/978-94-009-0511-5_209 contributor: fullname: Schröder – volume: 6 start-page: 4764 year: 2004 ident: 10.1016/j.bbabio.2014.01.013_bb0025 article-title: Evaluation of different mechanistic proposals for water oxidation in photosynthesis on the basis of Mn4OxCa structures for the catalytic site and spectroscopic data publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/b406437b contributor: fullname: Messinger – volume: 51 start-page: 6776 year: 2012 ident: 10.1016/j.bbabio.2014.01.013_bb0100 article-title: Determination of the miss probabilities of individual S-state transitions during photosynthetic water oxidation by monitoring electron flow in photosystem II using FTIR spectroscopy publication-title: Biochemistry doi: 10.1021/bi300708a contributor: fullname: Suzuki – volume: 72 start-page: 217 year: 2002 ident: 10.1016/j.bbabio.2014.01.013_bb0085 article-title: S-state dependence of the miss probability in photosystem II publication-title: Photosynth. Res. doi: 10.1023/A:1016128632704 contributor: fullname: de Wijn – volume: 81 start-page: 8094 year: 2009 ident: 10.1016/j.bbabio.2014.01.013_bb0120 article-title: Hydrogen peroxide production in the oxygen reduction reaction at different electrocatalysts as quantified by scanning electrochemical microscopy publication-title: Anal. Chem. doi: 10.1021/ac901291v contributor: fullname: Sanchez-Sanchez – volume: 1298 start-page: 180 year: 1996 ident: 10.1016/j.bbabio.2014.01.013_bb0210 article-title: Peroxidatic degradation of azide by catalase and irreversible enzyme inactivation publication-title: Biochim. Biophys. Acta doi: 10.1016/S0167-4838(96)00130-6 contributor: fullname: Lardinois – volume: 130 start-page: 3428 year: 2008 ident: 10.1016/j.bbabio.2014.01.013_bb0035 article-title: Quantum mechanics/molecular mechanics study of the catalytic cycle of water splitting in photosystem II publication-title: J. Am. Chem. Soc. doi: 10.1021/ja076130q contributor: fullname: Sproviero – volume: 252 start-page: 273 year: 2008 ident: 10.1016/j.bbabio.2014.01.013_bb0070 article-title: The manganese complex of photosystem II in its reaction cycle — basic framework and possible realization at the atomic level publication-title: Coord. Chem. Rev. doi: 10.1016/j.ccr.2007.09.001 contributor: fullname: Dau – volume: 29 start-page: 486 year: 1990 ident: 10.1016/j.bbabio.2014.01.013_bb0140 article-title: The S0 state of photosystem-II induced by hydroxylamine — differences between the structure of the manganese complex in the S0 and S1 states determined by X-ray absorption-spectroscopy publication-title: Biochemistry doi: 10.1021/bi00454a024 contributor: fullname: Guiles – volume: 502 start-page: 211 year: 1978 ident: 10.1016/j.bbabio.2014.01.013_bb0150 article-title: Photosynthetic oxygen evolution from hydrogen peroxide publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2728(78)90043-9 contributor: fullname: Velthuys – volume: 94 start-page: 247 year: 2007 ident: 10.1016/j.bbabio.2014.01.013_bb0240 article-title: Interactions of photosystem II with bicarbonate, formate and acetate publication-title: Photosynth. Res. doi: 10.1007/s11120-007-9200-2 contributor: fullname: Shevela – volume: 32 start-page: 9379 year: 1993 ident: 10.1016/j.bbabio.2014.01.013_bb0195 article-title: Generation, oxidation by the oxidized form of the tyrosine of polypeptide D2, and possible electronic configuration of the redox states S0, S−1, and S−2 of the water oxidase in isolated spinach thylakoids publication-title: Biochemistry doi: 10.1021/bi00087a017 contributor: fullname: Messinger – volume: 102 start-page: 487 year: 2009 ident: 10.1016/j.bbabio.2014.01.013_bb0055 article-title: Oxygen detection in biological systems publication-title: Photosynth. Res. doi: 10.1007/s11120-009-9434-2 contributor: fullname: Renger – volume: 36 start-page: 6862 year: 1997 ident: 10.1016/j.bbabio.2014.01.013_bb0250 article-title: S−3 state of the water oxidase in photosystem II publication-title: Biochemistry doi: 10.1021/bi962653r contributor: fullname: Messinger – volume: 1827 start-page: 1003 year: 2013 ident: 10.1016/j.bbabio.2014.01.013_bb0030 article-title: Water oxidation mechanism in photosystem II, including oxidations, proton release pathways, OO bond formation and O2 release publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbabio.2012.10.006 contributor: fullname: Siegbahn – volume: 109 start-page: 16035 year: 2012 ident: 10.1016/j.bbabio.2014.01.013_bb0075 article-title: Alternating electron and proton transfer steps in photosynthetic water oxidation publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1206266109 contributor: fullname: Klauss – volume: 936 start-page: 228 year: 1988 ident: 10.1016/j.bbabio.2014.01.013_bb0130 article-title: The reaction of hydrogen sulfide with the photosynthetic water oxidizing complex and its lack of reaction with the primary electron acceptor in spinach publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2728(88)90240-X contributor: fullname: Sivaraja – volume: 24 start-page: 123 year: 1972 ident: 10.1016/j.bbabio.2014.01.013_bb0235 article-title: Modulated light source use with the oxygen electrode publication-title: Methods Enzymol. doi: 10.1016/0076-6879(72)24062-9 contributor: fullname: Joliot – volume: 96 start-page: 4672 year: 2009 ident: 10.1016/j.bbabio.2014.01.013_bb0260 article-title: Two-electron reactions S2QB→S0QB and S3QB→S1QB are involved in deactivation of higher S states of the oxygen-evolving complex of photosystem II publication-title: Biophys. J. doi: 10.1016/j.bpj.2009.03.007 contributor: fullname: Antal – volume: 96 start-page: 2927 year: 1996 ident: 10.1016/j.bbabio.2014.01.013_bb0020 article-title: Manganese cluster in photosynthesis: where plants oxidize water to dioxygen publication-title: Chem. Rev. doi: 10.1021/cr950052k contributor: fullname: Yachandra – volume: 195 start-page: 133 year: 1952 ident: 10.1016/j.bbabio.2014.01.013_bb0230 article-title: A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)50881-X contributor: fullname: Beers – volume: 11 start-page: 457 year: 1970 ident: 10.1016/j.bbabio.2014.01.013_bb0060 article-title: Cooperation of charges in photosynthetic O2 evolution — a linear four step mechanism publication-title: Photochem. Photobiol. doi: 10.1111/j.1751-1097.1970.tb06017.x contributor: fullname: Kok – volume: 70 start-page: 3761 year: 1966 ident: 10.1016/j.bbabio.2014.01.013_bb0110 article-title: Role of hydrogen peroxide in reduction of oxygen at platinum electrodes publication-title: J. Phys. Chem. doi: 10.1021/j100883a515 contributor: fullname: Damjanov – volume: 26 start-page: 2495 year: 1987 ident: 10.1016/j.bbabio.2014.01.013_bb0165 article-title: Oxygen evolution from hydrogen-peroxide in photosystem II — flash-induced catalytic activity of water-oxidizing photosystem II membranes publication-title: Biochemistry doi: 10.1021/bi00383a014 contributor: fullname: Mano – volume: 105 start-page: 121 year: 1984 ident: 10.1016/j.bbabio.2014.01.013_bb0225 article-title: Catalase invitro publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(84)05016-3 contributor: fullname: Aebi – volume: 73 start-page: 149 year: 2002 ident: 10.1016/j.bbabio.2014.01.013_bb0200 article-title: The chequered history of the development and use of simultaneous equations for the accurate determination of chlorophylls a and b publication-title: Photosynth. Res. doi: 10.1023/A:1020470224740 contributor: fullname: Porra – volume: 2 start-page: 724 year: 2010 ident: 10.1016/j.bbabio.2014.01.013_bb0040 article-title: The mechanism of water oxidation: from electrolysis via homogeneous to biological catalysis publication-title: ChemCatChem doi: 10.1002/cctc.201000126 contributor: fullname: Dau – volume: 14 start-page: 7384 year: 2012 ident: 10.1016/j.bbabio.2014.01.013_bb0115 article-title: Hydrogen peroxide electrochemistry on platinum: towards understanding the oxygen reduction reaction mechanism publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/c2cp40616k contributor: fullname: Katsounaros – volume: 79 start-page: 544 year: 1977 ident: 10.1016/j.bbabio.2014.01.013_bb0220 article-title: Rapid, sensitive, and versatile assay for protein using coomassie brilliant blue G250 publication-title: Anal. Biochem. doi: 10.1016/0003-2697(77)90428-6 contributor: fullname: Sedmak – volume: 21 start-page: 438 year: 1965 ident: 10.1016/j.bbabio.2014.01.013_bb0190 article-title: Stoichiometry of photophosphorylation publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(65)90401-8 contributor: fullname: Winget – volume: 848 start-page: 359 year: 1986 ident: 10.1016/j.bbabio.2014.01.013_bb0175 article-title: H2O2 accessibility to the photosystem II donor side in protein-depleted inside-out thylakoids measured as flash-induced oxygen production publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2728(86)90211-2 contributor: fullname: Schröder – volume: 973 start-page: 23 year: 1989 ident: 10.1016/j.bbabio.2014.01.013_bb0180 article-title: H2O2 formation by photosystem II publication-title: Biochim. Biophys. Acta doi: 10.1016/S0005-2728(89)80397-4 contributor: fullname: Wydrzynski – volume: 36 start-page: 11055 year: 1997 ident: 10.1016/j.bbabio.2014.01.013_bb0145 article-title: Detection of an EPR multiline signal for the S0⁎ state in photosystem II publication-title: Biochemistry doi: 10.1021/bi9711285 contributor: fullname: Messinger – volume: 255 start-page: 74 year: 1992 ident: 10.1016/j.bbabio.2014.01.013_bb0010 article-title: The antiquity of oxygenic photosynthesis: evidence from stromatolites in sulphate-deficient Archaean lakes publication-title: Science doi: 10.1126/science.11536492 contributor: fullname: Buick – volume: 287 start-page: 13422 year: 2012 ident: 10.1016/j.bbabio.2014.01.013_bb0090 article-title: Misses during water oxidation in photosystem II are S-state dependent publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.342543 contributor: fullname: Han – volume: 277 start-page: 141 year: 1990 ident: 10.1016/j.bbabio.2014.01.013_bb0205 article-title: The reactivity of hydrazine with photosystem II strongly depends on the redox state of the water oxidizing system publication-title: FEBS lett. doi: 10.1016/0014-5793(90)80829-8 contributor: fullname: Messinger – volume: 72 start-page: 248 year: 1976 ident: 10.1016/j.bbabio.2014.01.013_bb0215 article-title: Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding publication-title: Anal. Biochem. doi: 10.1016/0003-2697(76)90527-3 contributor: fullname: Bradford – volume: 296 start-page: 1066 year: 2002 ident: 10.1016/j.bbabio.2014.01.013_bb0005 article-title: Life and the evolution of Earth's atmosphere publication-title: Science doi: 10.1126/science.1071184 contributor: fullname: Kasting – volume: 153 start-page: 625 year: 1968 ident: 10.1016/j.bbabio.2014.01.013_bb0050 article-title: A polarographic method for detection of oxygen production and reduction of hill reagent by isolated chloroplasts publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2728(68)90190-4 contributor: fullname: Joliot – volume: 8 start-page: 3460 year: 2006 ident: 10.1016/j.bbabio.2014.01.013_bb0245 article-title: Characterization of the water oxidizing complex of photosystem II of the Chl d-containing cyanobacterium Acaryochloris marina via its reactivity towards endogenous electron donors and acceptors publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/B604389E contributor: fullname: Shevela – volume: 936 start-page: 228 year: 1971 ident: 10.1016/j.bbabio.2014.01.013_bb0125 article-title: Action de faibles concentrations d'hydroxylamine sur l'emission d'oxygene des algues chlorella et des chloroplastes d'epinards publication-title: Biochim. Biophys. Acta contributor: fullname: Bouges – volume: 47 start-page: 11024 year: 2008 ident: 10.1016/j.bbabio.2014.01.013_bb0080 article-title: Monitoring water reactions during the S-state cycle of the photosynthetic water-oxidizing center: detection of the DOD bending vibrations by means of Fourier transform infrared spectroscopy publication-title: Biochemistry doi: 10.1021/bi801580e contributor: fullname: Suzuki – start-page: 111 year: 1977 ident: 10.1016/j.bbabio.2014.01.013_bb0135 contributor: fullname: Kok – volume: 53 start-page: 503 year: 2002 ident: 10.1016/j.bbabio.2014.01.013_bb0015 article-title: Complex evolution of photosynthesis publication-title: Annu. Rev. Plant Biol. doi: 10.1146/annurev.arplant.53.100301.135212 contributor: fullname: Xiong – volume: 42 start-page: 8929 year: 2003 ident: 10.1016/j.bbabio.2014.01.013_bb0095 article-title: Functional differences of photosystem II from Synechococcus elongatus and spinach characterized by flash induced oxygen evolution patterns publication-title: Biochemistry doi: 10.1021/bi034744b contributor: fullname: Isgandarova – volume: 30 start-page: 7852 year: 1991 ident: 10.1016/j.bbabio.2014.01.013_bb0255 article-title: Unusual low reactivity of the water oxidase in redox state S3 toward exogenous reductants — analysis of the NH2OH-induced and NH2NH2-induced modifications of flash-induced oxygen evolution in isolated spinach thylakoids publication-title: Biochemistry doi: 10.1021/bi00245a027 contributor: fullname: Messinger – volume: 891 start-page: 8 year: 1987 ident: 10.1016/j.bbabio.2014.01.013_bb0160 article-title: Hydrogen peroxide as an alternate substrate for the oxygen-evolving complex publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2728(87)90077-6 contributor: fullname: Frasch |
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| SubjectTerms | Electrochemistry hydrogen peroxide (H2O2) Hydrogen Peroxide - chemistry Manganese Oxygen - chemistry oxygen evolving complex (OEC) photosystem II (PSII) Photosystem II Protein Complex - chemistry Water oxidation |
| Title | Electrochemically produced hydrogen peroxide affects Joliot-type oxygen-evolution measurements of photosystem II |
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