| pubmed-article:11536737 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C0034865 | lld:lifeskim |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C1001877 | lld:lifeskim |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C0039476 | lld:lifeskim |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C1706211 | lld:lifeskim |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C0007961 | lld:lifeskim |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C1546426 | lld:lifeskim |
| pubmed-article:11536737 | lifeskim:mentions | umls-concept:C1548280 | lld:lifeskim |
| pubmed-article:11536737 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:11536737 | pubmed:dateCreated | 1997-8-31 | lld:pubmed |
| pubmed-article:11536737 | 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. | lld:pubmed |
| pubmed-article:11536737 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11536737 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11536737 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11536737 | pubmed:citationSubset | S | lld:pubmed |
| pubmed-article:11536737 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11536737 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11536737 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:11536737 | pubmed:issn | 0031-8655 | lld:pubmed |
| pubmed-article:11536737 | pubmed:author | pubmed-author:BlankenshipR... | lld:pubmed |
| pubmed-article:11536737 | pubmed:author | pubmed-author:ChiouH CHC | lld:pubmed |
| pubmed-article:11536737 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11536737 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:11536737 | pubmed:owner | NASA | lld:pubmed |
| pubmed-article:11536737 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11536737 | pubmed:pagination | 32-7 | lld:pubmed |
| pubmed-article:11536737 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:meshHeading | pubmed-meshheading:11536737... | lld:pubmed |
| pubmed-article:11536737 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:11536737 | pubmed:articleTitle | Temperature dependence of charge recombination in Heliobacillus mobilis. | lld:pubmed |
| pubmed-article:11536737 | pubmed:affiliation | Department of Chemistry and Biochemistry, Arizona State University, Tempe, USA. | lld:pubmed |
| pubmed-article:11536737 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11536737 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
