A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron

Hunter, ThérèseBonetta, RosalinSacco, AnthonyVella, MaritaSultana, Paul-MichaelTrinh, Chi H.Fadia, Hava B. R.Borowski, TomaszGarcía Fandiño, RebecaStockner, ThomasHunter, Gary J.2021-01-262021-01-262018T. 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, 5303http://hdl.handle.net/10347/24312We 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 ironeng© 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 madeAttribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/EnzymesIronManganeseMetalloproteinSuperoxide dismutaseA Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Ironjournal article10.1002/chem.2017046551521-3765open access