Halides inhibition of multicopper oxidases studied by FTIR spectroelectrochemistry using azide as an active infrared probe

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Halides inhibition of multicopper oxidases studied by FTIR spectroelectrochemistry using azide as an active infrared probe

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Publication Article, peer reviewed scientific
Title Halides inhibition of multicopper oxidases studied by FTIR spectroelectrochemistry using azide as an active infrared probe
Author Di Bari, Chiara ; Mano, Nicolas ; Pita, Marcos ; De Lacey, Antonio ; Shleev, Sergey
Research Centre Biofilms - Research Center for Biointerfaces
Date 2017
English abstract
An IR spectroelectrochem. study of Trametes hirsuta laccase and Magnaporthe oryzae bilirubin oxidase has been performed using azide, an inhibitor of multicopper oxidases, as an active IR probe incorporated into the T2​/T3 copper cluster of the enzymes. The redox potential-​controlled measurements indicate that N3-​ stretching IR bands of azide ion bound to the T2​/T3 cluster are only detected for the oxidized enzymes, confirming that azide only binds to Cu2+. Moreover, the process of binding​/dissocn. of azide ion is shown to be reversible. The interaction of halide anions, which also inhibit multicopper oxidases, with the active site of the enzymes was studied by measuring the changes in the azide FTIR bands. Enzymes inhibited by azide respond differently upon addn. of fluoride or chloride ions to the sample soln. inhibited by azide. Fluoride ions compete with azide for binding at one of the T2​/T3 Cu ions, whereas competition from chloride ions is much less evident.
DOI https://doi.org/10.1007/s00775-017-1494-8 (link to publisher's fulltext.)
Publisher Springer
Host/Issue Journal of biological inorganic chemistry : JBIC;8
Volume 22
ISSN 0949-8257
Language eng (iso)
Subject Sciences
Research Subject Categories::NATURAL SCIENCES
Handle http://hdl.handle.net/2043/24177 Permalink to this page
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