Ultrafast vibrational spectroscopy of the flavin chromophore

Minako Kondo; Jerôme Nappa; Kate L. Ronayne; Allison L. Stelling; Peter J. Tonge; Stephen R. Meech

doi:10.1021/jp0650735

Ultrafast vibrational spectroscopy of the flavin chromophore

Minako Kondo
, Jerôme Nappa
, Kate L. Ronayne
, Allison L. Stelling
, Peter J. Tonge
, Stephen R. Meech

Chemistry

University of East Anglia
STFC Rutherford Appleton Laboratory
Stony Brook University

Research output: Contribution to journal › Article › peer-review

66 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	20107-20110
Number of pages	4
Journal	Journal of Physical Chemistry B
Volume	110
Issue number	41
DOIs	https://doi.org/10.1021/jp0650735
State	Published - Oct 19 2006

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10.1021/jp0650735

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title = "Ultrafast vibrational spectroscopy of the flavin chromophore",

abstract = "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.",

author = "Minako Kondo and Jer{\^o}me Nappa and Ronayne, \{Kate L.\} and Stelling, \{Allison L.\} and Tonge, \{Peter J.\} and Meech, \{Stephen R.\}",

year = "2006",

month = oct,

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doi = "10.1021/jp0650735",

language = "English",

volume = "110",

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journal = "Journal of Physical Chemistry B",

issn = "1520-6106",

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TY - JOUR

T1 - Ultrafast vibrational spectroscopy of the flavin chromophore

AU - Kondo, Minako

AU - Nappa, Jerôme

AU - Ronayne, Kate L.

AU - Stelling, Allison L.

AU - Tonge, Peter J.

AU - Meech, Stephen R.

PY - 2006/10/19

Y1 - 2006/10/19

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/33751280484

U2 - 10.1021/jp0650735

DO - 10.1021/jp0650735

M3 - Article

AN - SCOPUS:33751280484

SN - 1520-6106

VL - 110

SP - 20107

EP - 20110

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 41

ER -

Ultrafast vibrational spectroscopy of the flavin chromophore

Abstract

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