Resonance Raman spectra of the neutral and anionic radical semiquinones of flavin adenine dinucleotide in glucose oxidase revisited

Johannes Schelvis, Doris Pun, Neelam Goyal, Olga Sokolova

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Flavin radical semiquinones are intermediates in important physiological processes. Resonance Raman (RR) spectroscopy is an important tool to determine the interactions between these radical intermediates and their protein environment that regulate their reactivity and role in the reaction mechanisms. RR spectra of flavin radical semiquinones have been available for several flavoproteins, and those in the glucose oxidase (GO) seem significantly different from all the other available data. Since GO is often used not only as a standard for flavin-containing proteins but also in biotechnological applications, we decided to reexamine the RR spectra of the neutral and anionic radical semiquinone forms of the flavin adenine dinucleotide (FAD) cofactor in this enzyme. The new data show that the vibrational wavenumbers of the neutral and anionic radical semiquinone forms of FAD in GO are very similar to those in other flavoproteins. The discrepancies that were observed earlier seem related to contributions of the FAD in different redox and protonation states. We also obtained the first RR spectra of the oxidized FAD cofactor in GO. Analysis of the vibrations of the oxidized FAD and its anionic radical semiquinone in GO in H2O and D2O solutions indicates that the subtle differences between these spectra in GO and in other flavoproteins are related to the weak hydrogen-bonding environment of the FAD cofactor in GO.

Original languageEnglish
Pages (from-to)822-829
Number of pages8
JournalJournal of Raman Spectroscopy
Volume37
Issue number8
DOIs
StatePublished - 1 Aug 2006

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Glucose Oxidase
Glucose oxidase
Flavin-Adenine Dinucleotide
Raman scattering
Flavoproteins
Proteins
Protonation
semiquinone radicals
Raman spectroscopy
Hydrogen bonds
Enzymes
4,6-dinitro-o-cresol

Keywords

  • Flavin radical semiquinone
  • Glucose oxidase
  • Resonance Raman spectroscopy

Cite this

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title = "Resonance Raman spectra of the neutral and anionic radical semiquinones of flavin adenine dinucleotide in glucose oxidase revisited",
abstract = "Flavin radical semiquinones are intermediates in important physiological processes. Resonance Raman (RR) spectroscopy is an important tool to determine the interactions between these radical intermediates and their protein environment that regulate their reactivity and role in the reaction mechanisms. RR spectra of flavin radical semiquinones have been available for several flavoproteins, and those in the glucose oxidase (GO) seem significantly different from all the other available data. Since GO is often used not only as a standard for flavin-containing proteins but also in biotechnological applications, we decided to reexamine the RR spectra of the neutral and anionic radical semiquinone forms of the flavin adenine dinucleotide (FAD) cofactor in this enzyme. The new data show that the vibrational wavenumbers of the neutral and anionic radical semiquinone forms of FAD in GO are very similar to those in other flavoproteins. The discrepancies that were observed earlier seem related to contributions of the FAD in different redox and protonation states. We also obtained the first RR spectra of the oxidized FAD cofactor in GO. Analysis of the vibrations of the oxidized FAD and its anionic radical semiquinone in GO in H2O and D2O solutions indicates that the subtle differences between these spectra in GO and in other flavoproteins are related to the weak hydrogen-bonding environment of the FAD cofactor in GO.",
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Resonance Raman spectra of the neutral and anionic radical semiquinones of flavin adenine dinucleotide in glucose oxidase revisited. / Schelvis, Johannes; Pun, Doris; Goyal, Neelam; Sokolova, Olga.

In: Journal of Raman Spectroscopy, Vol. 37, No. 8, 01.08.2006, p. 822-829.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Resonance Raman spectra of the neutral and anionic radical semiquinones of flavin adenine dinucleotide in glucose oxidase revisited

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AU - Pun, Doris

AU - Goyal, Neelam

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AB - Flavin radical semiquinones are intermediates in important physiological processes. Resonance Raman (RR) spectroscopy is an important tool to determine the interactions between these radical intermediates and their protein environment that regulate their reactivity and role in the reaction mechanisms. RR spectra of flavin radical semiquinones have been available for several flavoproteins, and those in the glucose oxidase (GO) seem significantly different from all the other available data. Since GO is often used not only as a standard for flavin-containing proteins but also in biotechnological applications, we decided to reexamine the RR spectra of the neutral and anionic radical semiquinone forms of the flavin adenine dinucleotide (FAD) cofactor in this enzyme. The new data show that the vibrational wavenumbers of the neutral and anionic radical semiquinone forms of FAD in GO are very similar to those in other flavoproteins. The discrepancies that were observed earlier seem related to contributions of the FAD in different redox and protonation states. We also obtained the first RR spectra of the oxidized FAD cofactor in GO. Analysis of the vibrations of the oxidized FAD and its anionic radical semiquinone in GO in H2O and D2O solutions indicates that the subtle differences between these spectra in GO and in other flavoproteins are related to the weak hydrogen-bonding environment of the FAD cofactor in GO.

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