1887

Abstract

possesses a pronounced extracellular Cu-reduction activity which leads to the accumulation of Cu in the medium. The kinetics of this reaction were not saturable by increasing copper concentrations, suggesting a non-enzymic reaction. A copper-reductase-deficient mutant, isolated by random transposon mutagenesis, had an insertion in the gene, which encodes -succinylbenzoic acid CoA ligase. This is a key enzyme in menaquinone biosynthesis. The Δ mutant was deficient in short-chain menaquinones, and exogenously added menaquinone complemented the copper-reductase-deficient phenotype. Haem-induced respiration of wild-type efficiently suppressed copper reduction, presumably by competition by the -type quinol oxidase for menaquinone. As expected, the Δ mutant was respiration-deficient, but could be made respiration-proficient by supplementation with menaquinone. Growth of wild-type cells was more copper-sensitive than that of the Δ mutant, due to the production of Cu ions by the wild-type. This growth inhibition of the wild-type was strongly attenuated if Cu was scavenged with the Cu(I) chelator bicinchoninic acid. These findings support a model whereby copper is non-enzymically reduced at the membrane by menaquinones. Respiration effectively competes for reduced quinones, which suppresses copper reduction. These findings highlight novel links between copper reduction, respiration and Cu toxicity in .

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2013-06-01
2022-01-24
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