Source:http://linkedlifedata.com/resource/pubmed/id/11536737
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-8-31
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pubmed:abstractText |
Transient absorption difference spectroscopy was used to study the temperature dependence of the P798+ decay kinetics in heliobacteria. For membrane samples, two components were obtained from the fitting of kinetic traces in the temperature range of 4-29 degrees C. A 3-9 ms component representing the cytochrome (cyt) c oxidation has an activation energy of 33.0 +/- 2.8 kJ/mol. A 12-22 ms component representing either P798+FX- or P798+FA/B- recombination has an activation energy of 15.3 +/- 2.4 kJ/mol. In isolated reaction centers (RC), only one 14 ms component due to P798+FX- recombination was obtained in this temperature range. The Arrhenius plot shows that the recombination rate of this P798+FX- state is temperature independent in the near room temperature range. For RC in the temperature range of 60-298 K, a 12-15 ms decay was obtained at temperatures greater than 240 K. Biphasic decay traces (12-15 ms and 2-4 ms components) were obtained at temperatures between 170 K and 230 K. Only one 2-4 ms component was found at temperatures lower than 160 K. The gradual switchover from the 12-15 ms to the 2-4 ms component upon cooling may indicate the shift of the P798+FX- recombination state to a state that is prior to P798+FX-, although other interpretations can not be excluded. The absorption difference spectrum (delta A @ 160 K - delta A @ 240 K) in the blue region shows a positive amplitude below 405 nm and a negative amplitude above 405 nm implying that the 2-4 ms decay component may be due to the recombination of P798+A1-, where A1 is a quinone-type acceptor.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
S
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0031-8655
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
64
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pubmed:owner |
NASA
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11536737-Bacteria,
pubmed-meshheading:11536737-Electrochemistry,
pubmed-meshheading:11536737-Electron Transport,
pubmed-meshheading:11536737-Energy Transfer,
pubmed-meshheading:11536737-Kinetics,
pubmed-meshheading:11536737-Light,
pubmed-meshheading:11536737-Photochemistry,
pubmed-meshheading:11536737-Photosynthesis,
pubmed-meshheading:11536737-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:11536737-Spectrophotometry,
pubmed-meshheading:11536737-Temperature
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pubmed:year |
1996
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pubmed:articleTitle |
Temperature dependence of charge recombination in Heliobacillus mobilis.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, Arizona State University, Tempe, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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