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Lookup NU author(s): Louisa Stewart,
Dr Kevin WaldronORCiD
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© 2019 The Royal Society of Chemistry. In bacteria, copper (Cu) is often recognised for its potential toxicity and its antibacterial activity is now considered a key component of the mammalian innate immune system. Cu ions bound in weak sites can catalyse harmful redox reactions while Cu ions in strong but adventitious sites can disrupt protein or enzyme function. For these reasons, the outward transport of Cu from bacteria has received significant attention. Yet, Cu is also a bacterial nutrient, required as a cofactor by enzymes that catalyse electron transfer processes, for instance in aerobic and anaerobic respiration. To date, the inward flow of this metal ion as a nutrient and its insertion into target cuproenzymes remain poorly defined. Here we revisit the available evidence related to bacterial nutrient Cu trafficking and identify gaps in knowledge. Particularly intriguing is the evidence that bacterial cuproenzymes do not always require auxiliary metallochaperones to insert nutrient Cu into their active sites. This review outlines our effort to consolidate the available experimental data using an established energy-driven model for metalation.
Author(s): Stewart LJ, Thaqi D, Kobe B, McEwan AG, Waldron KJ, Djoko KY
Publication type: Review
Publication status: Published
Print publication date: 01/01/2019
Online publication date: 10/10/2018
Acceptance date: 10/10/2018
ISSN (print): 1756-5901
ISSN (electronic): 1756-591X
Publisher: Royal Society of Chemistry
PubMed id: 30334058