Vibrational spectroscopy of flavoproteins

James N. Iuliano, Jarrod B. French, Peter J. Tonge

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations

Abstract

The flavin cofactor performs many functions in the cell based on the ability of the isoalloxazine ring to undergo one- or two-electron reduction and form covalent adducts with reactants such as amino acids. In addition, the strong visible absorption of the cofactor is also the basis for flavin-dependent photoreceptors. Vibrational spectroscopy is uniquely suited to studying the mechanism of flavoproteins since the frequency of the vibrational modes is very sensitive to the electronic structure and environment of the isoalloxazine ring. This chapter describes the mechanistic information that can be gained using vibrational spectroscopy as well experimental challenges and approaches that are used to obtain and interpret the complex data contained in a vibrational spectrum.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
EditorsBruce A. Palfey
PublisherAcademic Press Inc.
Pages189-214
Number of pages26
ISBN (Print)9780128168295
DOIs
StatePublished - 2019
Externally publishedYes

Publication series

NameMethods in Enzymology
Volume620
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • Blue light using FAD
  • Coherent anti-Stokes Raman spectroscopy
  • Density functional theory
  • Femtosecond stimulated Raman spectroscopy
  • Flavoenzyme
  • Flavoprotein photoreceptor
  • Fourier transform infrared spectroscopy
  • Glucose oxidase
  • Isoalloxazine ring
  • Light oxygen voltage domain
  • Old yellow enzyme
  • Photolyase
  • QM/MM
  • Raman spectroscopy
  • Resonance Raman spectroscopy
  • Riboflavin binding protein
  • Time-resolved infrared spectroscopy
  • Two-dimensional IR spectroscopy
  • Vibrational spectroscopy
  • p-Hydroxybenzoate hydroxylase

PubMed: MeSH publication types

  • Journal Article

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