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dc.contributor.author | Hunter, Thérèse |
dc.contributor.author | Bonetta, Rosalin |
dc.contributor.author | Sacco, Anthony |
dc.contributor.author | Vella, Marita |
dc.contributor.author | Sultana, Paul-Michael |
dc.contributor.author | Trinh, Chi H. |
dc.contributor.author | Fadia, Hava B. R. |
dc.contributor.author | Borowski, Tomasz |
dc.contributor.author | García Fandiño, Rebeca |
dc.contributor.author | Stockner, Thomas |
dc.contributor.author | Hunter, Gary J. |
dc.date.accessioned | 2021-01-26T07:58:26Z |
dc.date.available | 2021-01-26T07:58:26Z |
dc.date.issued | 2018 |
dc.identifier.citation | T. 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.uri | http://hdl.handle.net/10347/24312 |
dc.description.abstract | We 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.sponsorship | Work 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.iso | eng |
dc.publisher | Wiley |
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.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ |
dc.subject | Enzymes |
dc.subject | Iron |
dc.subject | Manganese |
dc.subject | Metalloprotein |
dc.subject | Superoxide dismutase |
dc.title | A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron |
dc.type | journal article |
dc.identifier.doi | 10.1002/chem.201704655 |
dc.relation.publisherversion | https://doi.org/10.1002/chem.201704655 |
dc.type.hasVersion | VoR |
dc.identifier.essn | 1521-3765 |
dc.rights.accessRights | open access |
dc.contributor.affiliation | Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares |
dc.contributor.affiliation | Universidade de Santiago de Compostela. Departamento de Química Orgánica |
dc.description.peerreviewed | SI |
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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
© 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