Electronic structure and hyperfine interactions in thioether-substituted tyrosyl radicals

Alexandre M. Boulet; Eric D. Walter; Dwight A. Schwartz; Gary J. Gerfen; Patrik R. Callis; David J. Singel

doi:10.1016/S0009-2614(00)01154-4

Electronic structure and hyperfine interactions in thioether-substituted tyrosyl radicals

Alexandre M. Boulet, Eric D. Walter, Dwight A. Schwartz, Gary J. Gerfen, Patrik R. Callis, David J. Singel

Physiology & Biophysics

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Electron-magnetic resonance spectroscopy and computational studies of the cysteine cross-linked tyrosyl radical in apogalactose oxidase have led to conflicting ideas regarding spectral assignments and protein-environment effects. We report DFT calculations on model radicals that clarify these issues. Calculated Fermi contact interactions do not resolve the ambiguity in spectral assignments; better insight is provided by the anisotropy of the hyperfine interactions and the systematic effects of thioether substitution. DFT results on model systems do not account for salient properties of the apogalactose radical. This inadequacy suggests that the protein environment exerts significant effects on the electronic structure of the radical.

Original language	English (US)
Pages (from-to)	108-114
Number of pages	7
Journal	Chemical Physics Letters
Volume	331
Issue number	1
DOIs	https://doi.org/10.1016/S0009-2614(00)01154-4
State	Published - Nov 24 2000

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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title = "Electronic structure and hyperfine interactions in thioether-substituted tyrosyl radicals",

abstract = "Electron-magnetic resonance spectroscopy and computational studies of the cysteine cross-linked tyrosyl radical in apogalactose oxidase have led to conflicting ideas regarding spectral assignments and protein-environment effects. We report DFT calculations on model radicals that clarify these issues. Calculated Fermi contact interactions do not resolve the ambiguity in spectral assignments; better insight is provided by the anisotropy of the hyperfine interactions and the systematic effects of thioether substitution. DFT results on model systems do not account for salient properties of the apogalactose radical. This inadequacy suggests that the protein environment exerts significant effects on the electronic structure of the radical.",

author = "Boulet, {Alexandre M.} and Walter, {Eric D.} and Schwartz, {Dwight A.} and Gerfen, {Gary J.} and Callis, {Patrik R.} and Singel, {David J.}",

note = "Funding Information: Computer resources used for these studies were acquired through grants from NSF (# DBI-9871191 and # DGE-9972824), and through a grant from Silicon Graphics Inc. We thank Gary D. Orser and Allison W. Banfield for technical assistance in the use of the SGI systems. Thoughtful contributions to this work from Professor Gerald T. Babcock are gratefully acknowledged. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.",

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doi = "10.1016/S0009-2614(00)01154-4",

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T1 - Electronic structure and hyperfine interactions in thioether-substituted tyrosyl radicals

AU - Boulet, Alexandre M.

AU - Walter, Eric D.

AU - Schwartz, Dwight A.

AU - Gerfen, Gary J.

AU - Callis, Patrik R.

AU - Singel, David J.

N1 - Funding Information: Computer resources used for these studies were acquired through grants from NSF (# DBI-9871191 and # DGE-9972824), and through a grant from Silicon Graphics Inc. We thank Gary D. Orser and Allison W. Banfield for technical assistance in the use of the SGI systems. Thoughtful contributions to this work from Professor Gerald T. Babcock are gratefully acknowledged. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 2000/11/24

Y1 - 2000/11/24

N2 - Electron-magnetic resonance spectroscopy and computational studies of the cysteine cross-linked tyrosyl radical in apogalactose oxidase have led to conflicting ideas regarding spectral assignments and protein-environment effects. We report DFT calculations on model radicals that clarify these issues. Calculated Fermi contact interactions do not resolve the ambiguity in spectral assignments; better insight is provided by the anisotropy of the hyperfine interactions and the systematic effects of thioether substitution. DFT results on model systems do not account for salient properties of the apogalactose radical. This inadequacy suggests that the protein environment exerts significant effects on the electronic structure of the radical.

AB - Electron-magnetic resonance spectroscopy and computational studies of the cysteine cross-linked tyrosyl radical in apogalactose oxidase have led to conflicting ideas regarding spectral assignments and protein-environment effects. We report DFT calculations on model radicals that clarify these issues. Calculated Fermi contact interactions do not resolve the ambiguity in spectral assignments; better insight is provided by the anisotropy of the hyperfine interactions and the systematic effects of thioether substitution. DFT results on model systems do not account for salient properties of the apogalactose radical. This inadequacy suggests that the protein environment exerts significant effects on the electronic structure of the radical.

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SP - 108

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JO - Chemical Physics Letters

JF - Chemical Physics Letters

IS - 1

ER -

Electronic structure and hyperfine interactions in thioether-substituted tyrosyl radicals

Abstract

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