2002
DOI: 10.1021/jp020356s
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Dynamic Conformations of Flavin Adenine Dinucleotide:  Simulated Molecular Dynamics of the Flavin Cofactor Related to the Time-Resolved Fluorescence Characteristics

Abstract: Molecular dynamics (MD) simulations and polarized subnanosecond time-resolved flavin fluorescence spectroscopy have been used to study the conformational dynamics of the flavin adenine dinucleotide (FAD) cofactor in aqueous solution. FAD displays a highly heterogeneous fluorescence intensity decay, resulting in lifetime spectra with two major components: a dominant 7-ps contribution that is characteristic of ultrafast fluorescence quenching and a 2.7-ns contribution resulting from moderate quenching. MD simula… Show more

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Cited by 134 publications
(173 citation statements)
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“…4 The remarkably low fluorescence yield of flavin adenine dinucleotide (FAD) with respect to free riboflavin was explained by the coplanar stacking of the flavin and adenine ring systems, most likely through a mechanism of photoinduced electron transfer of a nonfluorescent intramolecular ground-state complex between the isoalloxazine ring and the adenine moiety. 5 Binding of Rf to salycilate ion in aqueous solution was also reported to yield a nonfluorescent complex. 6 Besides the biological relevance of Rf, this molecule is usually present in water courses, lakes, and seas 7 and acts as a photosensitizer in the photo-oxidation of a range of contaminants through both Type I and Type II processes.…”
Section: ■ Introductionmentioning
confidence: 97%
“…4 The remarkably low fluorescence yield of flavin adenine dinucleotide (FAD) with respect to free riboflavin was explained by the coplanar stacking of the flavin and adenine ring systems, most likely through a mechanism of photoinduced electron transfer of a nonfluorescent intramolecular ground-state complex between the isoalloxazine ring and the adenine moiety. 5 Binding of Rf to salycilate ion in aqueous solution was also reported to yield a nonfluorescent complex. 6 Besides the biological relevance of Rf, this molecule is usually present in water courses, lakes, and seas 7 and acts as a photosensitizer in the photo-oxidation of a range of contaminants through both Type I and Type II processes.…”
Section: ■ Introductionmentioning
confidence: 97%
“…As shown in Fig. 4(A), the conformational transition from the native The intensity of FAD fluorescence remarkably increases when a FAD-containing protein is denatured with FAD gradually dissociated [16,17]. Acrylamide quenches the fluorescence of surfaceexposed and partially buried tryptophan residues but not those buried in the hydrophobic core of a protein.…”
Section: Resultsmentioning
confidence: 95%
“…FAD not only situates in the heart of the active site of XO and XDH, but is also a naturally fluorescent group-emitting green light [16]. The intensity of FAD fluorescence considerably increases when the protein has been denatured and can serve as a criterion of enzyme nativity [17].…”
Section: Introductionmentioning
confidence: 99%
“…26 However, a number of short lifetime components, on the order of tens of picoseconds, have also been reported. 27,28 The fluorescence lifetime of bound FAD is 0.3 ns, which is lower than that of free FAD. 29 The fluorescence lifetime values measured from FAD in our studies differ from some of the publications, but are in agreement with others.…”
Section: Introductionmentioning
confidence: 96%