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A charge polarization model for the metal-specific activity of superoxide dismutases

Lookup NU author(s): Dr Anna Barwinska-SendraORCiD, Dr Arnaud Basle, Dr Kevin WaldronORCiD



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


© 2018 the Owner Societies. The pathogenicity of Staphylococcus aureus is enhanced by having two superoxide dismutases (SODs): a Mn-specific SOD and another that can use either Mn or Fe. Using 94 GHz electron-nuclear double resonance (ENDOR) and electron double resonance detected (ELDOR)-NMR we show that, despite their different metal-specificities, their structural and electronic similarities extend down to their active-site 1H- and 14N-Mn(ii) hyperfine interactions. However these interactions, and hence the positions of these nuclei, are different in the inactive Mn-reconstituted Escherichia coli Fe-specific SOD. Density functional theory modelling attributes this to a different angular position of the E. coli H171 ligand. This likely disrupts the Mn-H171-E170′ triad causing a shift in charge and in metal redox potential, leading to the loss of activity. This is supported by the correlated differences in the Mn(ii) zero-field interactions of the three SOD types and suggests that the triad is important for determining metal specific activity.

Publication metadata

Author(s): Barwinska-Sendra A, Basle A, Waldron KJ, Un S

Publication type: Article

Publication status: Published

Journal: Physical Chemistry Chemical Physics

Year: 2018

Volume: 20

Issue: 4

Pages: 2363-2372

Print publication date: 28/01/2018

Online publication date: 18/12/2017

Acceptance date: 18/12/2017

Date deposited: 15/02/2018

ISSN (print): 1463-9076

ISSN (electronic): 1463-9084

Publisher: Royal Society of Chemistry


DOI: 10.1039/c7cp06829h


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Funder referenceFunder name
098375/Z/12/ZWellcome Trust