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Old dogs, new tricks: New insights into the iron/manganese superoxide dismutase family

Lookup NU author(s): Dr Kacper Sendra, Dr Kevin WaldronORCiD


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© 2022 Elsevier Inc. Superoxide dismutases (SODs) are ancient enzymes of widespread importance present in all domains of life. Many insights have been gained into these important enzymes over the 50 years since their initial description, but recent studies in the context of microbial pathogenesis have resulted in findings that challenge long established dogmas. The repertoire of SODs that bacterial pathogens encode is diverse both in number and in metal dependencies, including copper, copper and zinc, manganese, iron, and cambialistic enzymes. Other bacteria also possess nickel dependent SODs. Compartmentalization of SODs only partially explains their diversity. The need for pathogens to maintain SOD activity across distinct hostile environments encountered during infection, including those limited for essential metals, is also a driver of repertoire diversity. SOD research using pathogenic microbes has also revealed the apparent biochemical ease with which metal specificity can change within the most common family of SODs. Collectively, these studies are revealing the dynamic nature of SOD evolution, both that of individual SOD enzymes that can change their metal specificity to adapt to fluctuating cellular metal availability, and of a cell's repertoire of SOD isozymes that can be differentially expressed to adapt to fluctuating environmental metal availability in a niche.

Publication metadata

Author(s): Frye KA, Sendra KM, Waldron KJ, Kehl-Fie TE

Publication type: Article

Publication status: Published

Journal: Journal of Inorganic Biochemistry

Year: 2022

Volume: 230

Print publication date: 01/05/2022

Online publication date: 04/02/2022

Acceptance date: 30/01/2022

ISSN (print): 0162-0134

ISSN (electronic): 1873-3344

Publisher: Elsevier Inc.


DOI: 10.1016/j.jinorgbio.2022.111748


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