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EPR, ENDOR, and TRIPLE Resonance Spectroscopy on the Neutral Flavin Radical in

Title: EPR, ENDOR, and TRIPLE Resonance Spectroscopy on the Neutral Flavin Radical in
Authors: Escherichia Coli Dna; Christopher W. M. Kay; Richard Feicht; Kristina Schulz; Peter Sadewater; Aziz Sancar; Adelbert Bacher; Klaus Möbius; Gerald Richter; Stefan Weber
Contributors: The Pennsylvania State University CiteSeerX Archives
Source: http://www.physik.fu-berlin.de/~webers/kay_bc_38_16740.pdf.
Publication Year: 1999
Collection: CiteSeerX
Description: Ultraviolet radiation promotes the formation of a cyclobutane ring between adjacent pyrimidine residues on the same DNA strand to form a pyrimidine dimer. Such dimers may be restored to their monomeric forms through the action of a light-absorbing enzyme named DNA photolyase. The redoxactive cofactor involved in the light-induced electron transfer reactions of DNA repair and enzyme photoactivation is a noncovalently bound FAD. In this paper, the FAD cofactor of Escherichia coli DNA photolyase was characterized as the neutral flavin semiquinone by EPR spectroscopy at 9.68 and 94.5 GHz. From the high-frequency/high-field EPR spectrum, the principal values of the axially symmetric g-matrix of FADH . were extracted. Both EPR spectra show an emerging hyperfine splitting of 0.85 mT that could be assigned to the isotropic hyperfine coupling constant (hfc) of the proton at N(5). To obtain more information about the electron spin density distribution ENDOR and TRIPLE resonance spec.
Document Type: text
File Description: application/pdf
Language: English
Relation: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.21.9563
Availability: http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.21.9563; http://www.physik.fu-berlin.de/~webers/kay_bc_38_16740.pdf
Rights: Metadata may be used without restrictions as long as the oai identifier remains attached to it.
Accession Number: edsbas.C6DC6A21
Database: BASE