Fluorescence quenching of flavin adenine dinucleotide in aqueous solution by pH dependent isomerisation and photo-induced electron transfer

Islam, Shafiqul D.-M.; Susdorf, Thomas; Penzkofer, Alfons; Hegemann, Peter

doi:10.1016/j.chemphys.2003.08.013

Cited by 116 publications

(100 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…FAD allows studying the effect of dimer stacking, as dodecin traps FAD from solution in a closed conformation, forming a tryptophan-isoalloxazine-adenine-tryptophan instead of tryptophan-isoalloxazine-isoalloxazine-tryptophan aromatic tetrade (6). Steady-state and transient spectroscopy of FAD in solution demonstrated a quenching of the excited state of the flavin by interactions with the adenine subunit in the closed conformation (17,(45)(46)(47). If for the quenching mechanism the second aromatic moiety is important, one should notice a difference in the transient data for the different bound cofactors riboflavin and FAD, respectively.…”

Section: Resultsmentioning

confidence: 99%

Ultrafast Excited-state Deactivation of Flavins Bound to Dodecin

Staudt

Oesterhelt

Grininger

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Dodecin prevents riboflavin from autodegradation and exerting photo-induced cellular stress. Results: Ultrafast depopulation of excited states and ground state recovery is observed by transient spectroscopy. Conclusion: Ultrafast electron transfer in combination with proton transfer is responsible for deactivation of flavin excited states. Significance: A comprehensive study of parameters in the binding pocket affecting the riboflavin quenching mechanism is given.

show abstract

Section: Resultsmentioning

confidence: 99%

Ultrafast Excited-state Deactivation of Flavins Bound to Dodecin

Staudt

Oesterhelt

Grininger

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…This is the range of the fluorescence for flavins in aqueous solutions. 43 When gold colloids are present (at all the excitation wavelengths), the fluorescence band is relatively weak but so is the surface enhancement below 520 nm.…”

Section: Effect Of Fluorescencementioning

confidence: 99%

Surface‐enhanced Raman spectroscopy of bacteria: the effect of excitation wavelength and chemical modification of the colloidal milieu

Zeiri

Efrima

2005

J Raman Spectroscopy

View full text Add to dashboard Cite

Surface-enhanced Raman spectroscopy (SERS) of bacteria infused with silver or gold colloids reflects the different biochemicals in the immediate, nano-vicinity of the particles. In particular we demonstrate high sensitivity to flavins, important coenzymes usually associated with the cell wall. Varying the type of colloid, the laser excitation wavelength and the chemical protocols enables us to observe spectral signatures from different biochemical components of the microorganism. Specifically, we can switch between normal Raman, resonance Raman, and SERS, altering the relative spectral contributions of the various cell constituents.

show abstract

“…[1][2][3][4] Time-resolved fluorescence measurements fully confirmed this early model of closed FAD. [5][6][7][8][9] However, structural investigations have always been an object of dispute. Indeed, X-ray structural access to closed FAD is difficult due to the inherent flexibility and conformational dynamics of FAD.…”

Section: Introductionmentioning

confidence: 99%