Ultrafast Vibrational Spectroscopy of the Flavin Chromophore

Ultrafast time-resolved infrared (TRIR) spectra of flavin adenine dinucleotide (FAD) and the anion of lumiflavin (Lf-) are described. Ground-state recovery and excited-state decay of FAD reveal a common dominant ultrafast relaxation and a minor slower component. The Lf- transient lacks a fast compon...

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Bibliographic Details
Published inThe journal of physical chemistry. B Vol. 110; no. 41; pp. 20107 - 20110
Main Authors Kondo, Minako, Nappa, Jérôme, Ronayne, Kate L, Stelling, Allison L, Tonge, Peter J, Meech, Stephen R
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 19.10.2006
Subjects
Anions
Chemistry, Physical - methods
Flavins - chemistry
Kinetics
Models, Chemical
Models, Statistical
Normal Distribution
Photochemistry - methods
Spectrophotometry - methods
Spectrophotometry, Infrared - methods
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Summary:Ultrafast time-resolved infrared (TRIR) spectra of flavin adenine dinucleotide (FAD) and the anion of lumiflavin (Lf-) are described. Ground-state recovery and excited-state decay of FAD reveal a common dominant ultrafast relaxation and a minor slower component. The Lf- transient lacks a fast component. No intermediate species are observed, suggesting that the quenching mechanism is internal conversion promoted by interaction of the adenine and isoalloxazine rings in FAD. Modes are assigned, and the potential for extension of the TRIR method to photoactive proteins is discussed.
Bibliography:ark:/67375/TPS-5V7LJRDT-Z
istex:47D3467577EEF580EC923DAF449FE23EDC928086
SourceType-Other Sources-1
ObjectType-Article-2
content type line 63
ObjectType-Correspondence-1
ISSN:1520-6106
1520-5207
DOI:10.1021/jp0650735