Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides
Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modifi...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Espiritu, Eduardo [verfasserIn] Chamberlain, Kori D. [verfasserIn] Williams, JoAnn C. [verfasserIn] Allen, James P. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Photosynthesis research - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1980, 143(2019), 2 vom: 22. Okt., Seite 129-141 |
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| Übergeordnetes Werk: |
volume:143 ; year:2019 ; number:2 ; day:22 ; month:10 ; pages:129-141 |
| Links: |
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| DOI / URN: |
10.1007/s11120-019-00680-3 |
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| Katalog-ID: |
SPR017110246 |
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| 245 | 1 | 0 | |a Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides |
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| 520 | |a Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. | ||
| 650 | 4 | |a Bacterial reaction centers |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Optical spectroscopy |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Electron transfer |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Secondary electron donors |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Mn-cofactors |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Chamberlain, Kori D. |e verfasserin |4 aut | |
| 700 | 1 | |a Williams, JoAnn C. |e verfasserin |4 aut | |
| 700 | 1 | |a Allen, James P. |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Photosynthesis research |d Dordrecht [u.a.] : Springer Science + Business Media B.V, 1980 |g 143(2019), 2 vom: 22. Okt., Seite 129-141 |w (DE-627)269758410 |w (DE-600)1475688-2 |x 1573-5079 |7 nnns |
| 773 | 1 | 8 | |g volume:143 |g year:2019 |g number:2 |g day:22 |g month:10 |g pages:129-141 |
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2019 |
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10.1007/s11120-019-00680-3 doi (DE-627)SPR017110246 (SPR)s11120-019-00680-3-e DE-627 ger DE-627 rakwb eng 580 540 ASE 35.00 bkl 42.00 bkl Espiritu, Eduardo verfasserin aut Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. Bacterial reaction centers (dpeaa)DE-He213 Optical spectroscopy (dpeaa)DE-He213 Electron transfer (dpeaa)DE-He213 Secondary electron donors (dpeaa)DE-He213 Mn-cofactors (dpeaa)DE-He213 Chamberlain, Kori D. verfasserin aut Williams, JoAnn C. verfasserin aut Allen, James P. verfasserin aut Enthalten in Photosynthesis research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1980 143(2019), 2 vom: 22. Okt., Seite 129-141 (DE-627)269758410 (DE-600)1475688-2 1573-5079 nnns volume:143 year:2019 number:2 day:22 month:10 pages:129-141 https://dx.doi.org/10.1007/s11120-019-00680-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 42.00 ASE AR 143 2019 2 22 10 129-141 |
| spelling |
10.1007/s11120-019-00680-3 doi (DE-627)SPR017110246 (SPR)s11120-019-00680-3-e DE-627 ger DE-627 rakwb eng 580 540 ASE 35.00 bkl 42.00 bkl Espiritu, Eduardo verfasserin aut Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. Bacterial reaction centers (dpeaa)DE-He213 Optical spectroscopy (dpeaa)DE-He213 Electron transfer (dpeaa)DE-He213 Secondary electron donors (dpeaa)DE-He213 Mn-cofactors (dpeaa)DE-He213 Chamberlain, Kori D. verfasserin aut Williams, JoAnn C. verfasserin aut Allen, James P. verfasserin aut Enthalten in Photosynthesis research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1980 143(2019), 2 vom: 22. Okt., Seite 129-141 (DE-627)269758410 (DE-600)1475688-2 1573-5079 nnns volume:143 year:2019 number:2 day:22 month:10 pages:129-141 https://dx.doi.org/10.1007/s11120-019-00680-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 42.00 ASE AR 143 2019 2 22 10 129-141 |
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10.1007/s11120-019-00680-3 doi (DE-627)SPR017110246 (SPR)s11120-019-00680-3-e DE-627 ger DE-627 rakwb eng 580 540 ASE 35.00 bkl 42.00 bkl Espiritu, Eduardo verfasserin aut Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. Bacterial reaction centers (dpeaa)DE-He213 Optical spectroscopy (dpeaa)DE-He213 Electron transfer (dpeaa)DE-He213 Secondary electron donors (dpeaa)DE-He213 Mn-cofactors (dpeaa)DE-He213 Chamberlain, Kori D. verfasserin aut Williams, JoAnn C. verfasserin aut Allen, James P. verfasserin aut Enthalten in Photosynthesis research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1980 143(2019), 2 vom: 22. Okt., Seite 129-141 (DE-627)269758410 (DE-600)1475688-2 1573-5079 nnns volume:143 year:2019 number:2 day:22 month:10 pages:129-141 https://dx.doi.org/10.1007/s11120-019-00680-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 42.00 ASE AR 143 2019 2 22 10 129-141 |
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10.1007/s11120-019-00680-3 doi (DE-627)SPR017110246 (SPR)s11120-019-00680-3-e DE-627 ger DE-627 rakwb eng 580 540 ASE 35.00 bkl 42.00 bkl Espiritu, Eduardo verfasserin aut Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. Bacterial reaction centers (dpeaa)DE-He213 Optical spectroscopy (dpeaa)DE-He213 Electron transfer (dpeaa)DE-He213 Secondary electron donors (dpeaa)DE-He213 Mn-cofactors (dpeaa)DE-He213 Chamberlain, Kori D. verfasserin aut Williams, JoAnn C. verfasserin aut Allen, James P. verfasserin aut Enthalten in Photosynthesis research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1980 143(2019), 2 vom: 22. Okt., Seite 129-141 (DE-627)269758410 (DE-600)1475688-2 1573-5079 nnns volume:143 year:2019 number:2 day:22 month:10 pages:129-141 https://dx.doi.org/10.1007/s11120-019-00680-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 42.00 ASE AR 143 2019 2 22 10 129-141 |
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10.1007/s11120-019-00680-3 doi (DE-627)SPR017110246 (SPR)s11120-019-00680-3-e DE-627 ger DE-627 rakwb eng 580 540 ASE 35.00 bkl 42.00 bkl Espiritu, Eduardo verfasserin aut Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. Bacterial reaction centers (dpeaa)DE-He213 Optical spectroscopy (dpeaa)DE-He213 Electron transfer (dpeaa)DE-He213 Secondary electron donors (dpeaa)DE-He213 Mn-cofactors (dpeaa)DE-He213 Chamberlain, Kori D. verfasserin aut Williams, JoAnn C. verfasserin aut Allen, James P. verfasserin aut Enthalten in Photosynthesis research Dordrecht [u.a.] : Springer Science + Business Media B.V, 1980 143(2019), 2 vom: 22. Okt., Seite 129-141 (DE-627)269758410 (DE-600)1475688-2 1573-5079 nnns volume:143 year:2019 number:2 day:22 month:10 pages:129-141 https://dx.doi.org/10.1007/s11120-019-00680-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 35.00 ASE 42.00 ASE AR 143 2019 2 22 10 129-141 |
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Enthalten in Photosynthesis research 143(2019), 2 vom: 22. Okt., Seite 129-141 volume:143 year:2019 number:2 day:22 month:10 pages:129-141 |
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Enthalten in Photosynthesis research 143(2019), 2 vom: 22. Okt., Seite 129-141 volume:143 year:2019 number:2 day:22 month:10 pages:129-141 |
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Bacterial reaction centers Optical spectroscopy Electron transfer Secondary electron donors Mn-cofactors |
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Photosynthesis research |
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Espiritu, Eduardo @@aut@@ Chamberlain, Kori D. @@aut@@ Williams, JoAnn C. @@aut@@ Allen, James P. @@aut@@ |
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The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. 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Espiritu, Eduardo |
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Espiritu, Eduardo ddc 580 bkl 35.00 bkl 42.00 misc Bacterial reaction centers misc Optical spectroscopy misc Electron transfer misc Secondary electron donors misc Mn-cofactors Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides |
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580 540 ASE 35.00 bkl 42.00 bkl Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides Bacterial reaction centers (dpeaa)DE-He213 Optical spectroscopy (dpeaa)DE-He213 Electron transfer (dpeaa)DE-He213 Secondary electron donors (dpeaa)DE-He213 Mn-cofactors (dpeaa)DE-He213 |
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Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides |
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Elektronische Aufsätze |
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Espiritu, Eduardo |
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10.1007/s11120-019-00680-3 |
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bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from rhodobacter sphaeroides |
| title_auth |
Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides |
| abstract |
Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. |
| abstractGer |
Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. |
| abstract_unstemmed |
Abstract A biohybrid model system is described that interfaces synthetic Mn-oxides with bacterial reaction centers to gain knowledge concerning redox reactions by metal clusters in proteins, in particular the $ Mn_{4} %$ CaO_{5} $ cluster of photosystem II. The ability of Mn-oxides to bind to modified bacterial reaction centers and transfer an electron to the light-induced oxidized bacteriochlorophyll dimer, $ P^{+} $, was characterized using optical spectroscopy. The environment of P was altered to obtain a high P/$ P^{+} $ midpoint potential. In addition, different metal-binding sites were introduced by substitution of amino acid residues as well as extension of the C-terminus of the M subunit with the C-terminal region of the D1 subunit of photosystem II. The Mn-compounds $ MnO_{2} $, $ αMn_{2} %$ O_{3} $, $ Mn_{3} %$ O_{4} $, $ CaMn_{2} %$ O_{4} $, and $ Mn_{3} $($ PO_{4} $)2 were tested and compared to $ MnCl_{2} $. In general, addition of the Mn-compounds resulted in a decrease in the amount of $ P^{+} $ while the reduced quinone was still present, demonstrating that the Mn-compounds can serve as secondary electron donors. The extent of $ P^{+} $ reduction for the Mn-oxides was largest for $ αMn_{2} %$ O_{3} $ and $ CaMn_{2} %$ O_{4} $ and smallest for $ Mn_{3} %$ O_{4} $ and $ MnO_{2} $. The addition of $ Mn_{3} $($ PO_{4} $)2 resulted in nearly complete $ P^{+} $ reduction, similar to $ MnCl_{2} $. Overall, the activity was correlated with the initial oxidation state of the Mn-compound. Transient optical measurements showed a fast kinetic component, assigned to reduction of $ P^{+} $ by the Mn-oxide, in addition to a slow component due to charge recombination. The results support the conjecture that the incorporation of Mn-oxides by ancient anoxygenic phototrophs was a step in the evolution of oxygenic photosynthesis. |
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Bound manganese oxides capable of reducing the bacteriochlorophyll dimer of modified reaction centers from Rhodobacter sphaeroides |
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Chamberlain, Kori D. Williams, JoAnn C. Allen, James P. |
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| score |
7.403097 |