An evolutionary path to altered cofactor specificity in a metalloenzyme

Anna Barwinska-Sendra, Yuritzi M. Garcia, Kacper M. Sendra, Arnaud Baslé, Eilidh S. Mackenzie, Emma Tarrant, Patrick Card, Leandro C. Tabares, Cédric Bicep, Sun Un, Thomas E. Kehl-Fie () and Kevin J. Waldron ()
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Anna Barwinska-Sendra: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University
Yuritzi M. Garcia: Department of Microbiology, University of Illinois Urbana-Champaign
Kacper M. Sendra: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University
Arnaud Baslé: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University
Eilidh S. Mackenzie: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University
Emma Tarrant: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University
Patrick Card: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University
Leandro C. Tabares: Department of Biochemistry, Biophysics and Structural Biology, Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC)
Cédric Bicep: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University
Sun Un: Department of Biochemistry, Biophysics and Structural Biology, Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC)
Thomas E. Kehl-Fie: Department of Microbiology, University of Illinois Urbana-Champaign
Kevin J. Waldron: Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University

Nature Communications, 2020, vol. 11, issue 1, 1-13

Abstract: Abstract Almost half of all enzymes utilize a metal cofactor. However, the features that dictate the metal utilized by metalloenzymes are poorly understood, limiting our ability to manipulate these enzymes for industrial and health-associated applications. The ubiquitous iron/manganese superoxide dismutase (SOD) family exemplifies this deficit, as the specific metal used by any family member cannot be predicted. Biochemical, structural and paramagnetic analysis of two evolutionarily related SODs with different metal specificity produced by the pathogenic bacterium Staphylococcus aureus identifies two positions that control metal specificity. These residues make no direct contacts with the metal-coordinating ligands but control the metal’s redox properties, demonstrating that subtle architectural changes can dramatically alter metal utilization. Introducing these mutations into S. aureus alters the ability of the bacterium to resist superoxide stress when metal starved by the host, revealing that small changes in metal-dependent activity can drive the evolution of metalloenzymes with new cofactor specificity.

Date: 2020
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DOI: 10.1038/s41467-020-16478-0

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