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  Insights into the nature of the hydrogen bonding of ·Tyr272 in apo-galactose oxidase

Benisvy, L., Hammond, D., Parker, D. J., Davies, E. S., Garner, C. D., McMaster, J., et al. (2007). Insights into the nature of the hydrogen bonding of ·Tyr272 in apo-galactose oxidase. Journal of Inorganic Biochemistry, 101(11-12), 1859-1864. doi:10.1016/j.jinorgbio.2007.07.013.

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 Creators:
Benisvy, Laurent1, Author           
Hammond, Deborah2, Author
Parker, David J.2, Author
Davies, E. Stephen2, Author
Garner, C. David2, Author
McMaster, Jonathan2, Author
Wilson, Claire2, Author
Neese, Frank1, 3, Author           
Bothe, Eberhard1, Author           
Bittl, Robert4, Author
Teutloff, Christian4, Author
Affiliations:
1Research Department Wieghardt, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society, ou_3023881              
2School of Chemistry, The University of Nottingham, University Park, Nottingham, NG7 2RD, UK, ou_persistent22              
3Institut für Physikalische and Theoretische Chemie, Universität Bonn, Wegelerstrasse 12, D-53115 Bonn, Germany, ou_persistent22              
4Institut für Experimentalphysik, Freie Universität, Berlin, Arnimallee 14,14195 Berlin, Germany, ou_persistent22              

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Free keywords: Oxidized apo-galactose oxidase; Density functional calculations; Electronic structure; EPR spectroscopy; Hydrogen bond; Thioether phenoxyl radical
 Abstract: The synthesis and structure of an o-methylthio-phenol-imidazole, 2-(2′-(4′-tert-butyl-6′-methylsulfanyl)-hydroxyphenyl))-4,5-diphenyl-imidazole (MeSLH), is reported; X-ray crystallographic studies have shown that MeSLH involves an O–H···N+ hydrogen bond between the phenol and an imidazole nitrogen. MeSLH undergoes a reversible, one-electron, oxidation to form the radical cation [MeSLH]·+ the EPR spectrum of which is remarkably similar to that of ·Tyr272 in Cu-free, oxidized, apo-GO. Density Functional Theory calculations, have shown that the proton-transferred (R–O····H–N+) form of [MeSLH]·+ has a spin density distribution – with a substantial delocalization of the unpaired electron spin density onto the ortho sulfur atom – and EPR properties that are in good agreement with those of ·Tyr272 in Cu-free, oxidized, apo-GO whereas the non-proton-transferred (R–O·+–H···N) form does not. The results reported herein are a further demonstration of the influence of hydrogen bonding on the nature and properties of phenoxyl radicals and strongly suggest that the phenoxyl oxygen of ·Tyr272 in Cu-free, oxidized, apo-GO is involved in a O····H–O/N hydrogen bond.

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Language(s): eng - English
 Dates: 2007-04-162007-07-212007-11-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jinorgbio.2007.07.013
 Degree: -

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Title: Journal of Inorganic Biochemistry
  Abbreviation : J. Inorg. Biochem.
Source Genre: Journal
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Publ. Info: New York : Elsevier
Pages: - Volume / Issue: 101 (11-12) Sequence Number: - Start / End Page: 1859 - 1864 Identifier: ISSN: 0162-0134
CoNE: https://pure.mpg.de/cone/journals/resource/954925478535