Related Experiment Video
Updated: Jul 19, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
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.
More Related Videos
Related Concept Videos
UV–Vis Spectroscopy: Molecular Electronic Transitions
Ultraviolet and Visible (UV–Vis) Spectroscopy: Overview
IR and UV–Vis Spectroscopy of Aldehydes and Ketones
Atomic Fluorescence Spectroscopy
UV–Vis Spectroscopy of Conjugated Systems
One of the factors influencing λmax is the extent of conjugation in the...
UV–Vis Spectrometers

