Source:http://linkedlifedata.com/resource/pubmed/id/17474766
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
2007-5-17
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pubmed:abstractText |
Ultrafast fluorescence quenching of flavin in flavodoxin from Megasphaera elsdenii was investigated by means of a fluorescence up-conversion method. Fluorescence lifetimes of flavodoxin from M. elsdenii were estimated to be tau(1) approximately 165 fs (0.97%) and tau(2) approximately 10 ps (0.03%). Correlation of photoinduced electron-transfer rates (k(ET)) with averaged distances (D(av)) between isoalloxazine and nearby tryptophan or tyrosine was examined and obtained an empirical equation of ln k(ET) vs D(av) by means of a nonlinear least-squares method using reported data together with flavodoxin from M. elsdenii. The values of D(av) were calculated from X-ray structures of the flavoproteins. The ln k(ET) was approximately linear at D(av) shorter than 7 A. The model free empirical equation was expressed as ln k(ET) = 29.7 + (-0.327 D(av) + 2.84 x 10(-5))/(0.698 - D(av)(2)). We also analyzed the observed values of ln k(ET) with Marcus theory, but could not obtain reasonable results. Our analysis suggests that the average distance, rather than the shortest (edge to edge) distance or interplanar angles between the aromatics rings, is the key factor in the process of the photoinduced electron transfer in these flavoproteins.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acyl-CoA Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Flavins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavodoxin,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/isoalloxazine,
http://linkedlifedata.com/resource/pubmed/chemical/riboflavin-binding protein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1520-6106
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
111
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5694-9
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pubmed:meshHeading |
pubmed-meshheading:17474766-Acyl-CoA Dehydrogenase,
pubmed-meshheading:17474766-Electron Transport,
pubmed-meshheading:17474766-Flavins,
pubmed-meshheading:17474766-Flavodoxin,
pubmed-meshheading:17474766-Glucose Oxidase,
pubmed-meshheading:17474766-Membrane Transport Proteins,
pubmed-meshheading:17474766-Models, Molecular,
pubmed-meshheading:17474766-Photochemistry,
pubmed-meshheading:17474766-Protein Conformation,
pubmed-meshheading:17474766-Tryptophan,
pubmed-meshheading:17474766-Tyrosine
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pubmed:year |
2007
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pubmed:articleTitle |
Donor-acceptor distance-dependence of photoinduced electron-transfer rate in flavoproteins.
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pubmed:affiliation |
SC1-414 Department of Chemistry, Faculty of Science, Mahasarakham University, Mahasarakham 44150, Thailand. fukoh2003@yahoo.com
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pubmed:publicationType |
Journal Article
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