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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1980-12-16
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pubmed:abstractText |
The resonance Raman (RR) spectra of semiquinones of complexes of riboflavin or 8-methoxyriboflavin (8-OCH3-RF) with riboflavin binding protein (RBP) were observed. The RR spectrum of neutral semiquinone of riboflavin-RBP complex in H2O solution has an intense line at 1617 cm-1, not observed for oxidized riboflavin bound to RBP. The line at 1617 cm-1 does not shift in D2O solution. The absorption spectrum of semiquinone of 8-OCH3-RF bound to RBP has maxima at 586, 396, and 344 nm, and the RR spectrum doublet lines at 1623 and 1615 cm-1. In D2O solution, the 1623 cm-1 line does not shift, but the 1615 cm-1 line shifts to 1604 cm-1. The line around 1620 cm-1 for the flavin semiquinone will be useful in the determination of the redox state of flavin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
411-6
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:7419502-Binding Sites,
pubmed-meshheading:7419502-Carrier Proteins,
pubmed-meshheading:7419502-Egg White,
pubmed-meshheading:7419502-Membrane Transport Proteins,
pubmed-meshheading:7419502-Oxidation-Reduction,
pubmed-meshheading:7419502-Protein Binding,
pubmed-meshheading:7419502-Protein Conformation,
pubmed-meshheading:7419502-Riboflavin,
pubmed-meshheading:7419502-Spectrophotometry,
pubmed-meshheading:7419502-Spectrum Analysis, Raman,
pubmed-meshheading:7419502-Structure-Activity Relationship
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pubmed:year |
1980
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pubmed:articleTitle |
Resonance Raman spectra of semiquinone forms of flavins bound to riboflavin binding protein.
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pubmed:publicationType |
Journal Article
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