Hunter, T, Bonetta, R, Sacco, A et al. (8 more authors) (2018) A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron. Chemistry - A European Journal, 24 (20). pp. 5303-5308. ISSN 0947-6539
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 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. |
Keywords: | enzymes; iron; manganese; metalloprotein; superoxide dismutase |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Synthetic Biology (Leed) |
Depositing User: | Symplectic Publications |
Date Deposited: | 10 Oct 2018 11:20 |
Last Modified: | 02 Jan 2019 14:33 |
Status: | Published |
Publisher: | Wiley |
Identification Number: | 10.1002/chem.201704655 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:136900 |