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dc.contributor.authorHunter, Thérèse
dc.contributor.authorBonetta, Rosalin
dc.contributor.authorSacco, Anthony
dc.contributor.authorVella, Marita
dc.contributor.authorSultana, Paul-Michael
dc.contributor.authorTrinh, Chi H.
dc.contributor.authorFadia, Hava B. R.
dc.contributor.authorBorowski, Tomasz
dc.contributor.authorGarcía Fandiño, Rebeca
dc.contributor.authorStockner, Thomas
dc.contributor.authorHunter, Gary J.
dc.date.accessioned2021-01-26T07:58:26Z
dc.date.available2021-01-26T07:58:26Z
dc.date.issued2018
dc.identifier.citationT. Hunter, R. Bonetta, A. Sacco, M. Vella, P.-M. Sultana, C. H. Trinh, H. B. R. Fadia, T. Borowski, R. Garcia-Fandiño, T. Stockner, G. J. Hunter, Chem. Eur. J. 2018, 24, 5303
dc.identifier.urihttp://hdl.handle.net/10347/24312
dc.description.abstractWe have generated a site‐directed mutant of the manganese superoxide dismutase SOD‐3 of C.elegans (MnSOD‐3) which modifies the metal specificity of the enzyme. While wild‐type MnSOD‐3 functions with manganese in the active site (3600 U mg−1 of protein) it has little or no activity when iron is incorporated. However, when histidine replaces glutamine 142 in the active site, the enzyme retains 50 % of its activity and becomes cambialistic for its metal cofactor exhibiting very similar specific activity with either manganese or iron
dc.description.sponsorshipWork reported here was carried out using funding from UoM grants PHBIN02‐1, PHBRP03‐05 and PHBRP03‐17. The European Union Erasmus+ programme (project number: 2016‐1‐PL01‐KA103‐023786) is acknowledged for providing financial support for the mobility traineeship of T.B. This research was supported in part by PL‐Grid Infrastructure. We wish to thank the EU COST association for support through COST actions CM1305 and CM1306
dc.language.isoeng
dc.publisherWiley
dc.rights© 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectEnzymes
dc.subjectIron
dc.subjectManganese
dc.subjectMetalloprotein
dc.subjectSuperoxide dismutase
dc.titleA Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron
dc.typejournal article
dc.identifier.doi10.1002/chem.201704655
dc.relation.publisherversionhttps://doi.org/10.1002/chem.201704655
dc.type.hasVersionVoR
dc.identifier.essn1521-3765
dc.rights.accessRightsopen access
dc.contributor.affiliationUniversidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares
dc.contributor.affiliationUniversidade de Santiago de Compostela. Departamento de Química Orgánica
dc.description.peerreviewedSI


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© 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.  This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made
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 © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution‐NonCommercial‐NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made





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