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Superhero superoxide dismutase (360.2)
Author(s) -
Culotta Val
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.360.2
Subject(s) - superoxide dismutase , pathogen , microbiology and biotechnology , enzyme , reactive oxygen species , biology , biochemistry , chemistry
From archaic bacteria to humans, the superoxide dismutase (SOD) metallo enzymes play important roles in controlling reactive oxygen species. SOD enzymes fall into three classes based on metal co‐factor used: (i) copper, (II) nickel or (iii) iron/manganese. These three classes are completely unrelated in sequence but have converged in evolution to catalyze the disproportionation of superoxide at rates limited only by diffusion. Like all metalloproteins, SOD enzymes face the challenges of acquiring the proper metal co‐factor under conditions of limited metal availability and in a sea of competing non‐cofactor metals. This issue is particularly problematic at the host‐pathogen interface, where the host attempts to starve the pathogen of certain essential metals and bombard with toxic levels of other metals. In spite of these harsh metal conditions, pathogenic bacteria and fungi manage to properly activate their SODs with the correct metal co‐factor and combat the oxidative burst of host immunity. Two such examples include the Lyme disease pathogen Borrelia burgorferi and the infectious yeast Candida albicans. Both organisms have evolved with a novel family of SOD enzymes and metal homeostasis mechanisms that ensure SOD enzyme activation at the host‐pathogen interface. These adaptations in metals and SOD enzymes will be the focus of discussion.