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Significance Copper is particularly important in the metabolism of methanotrophs, methane-consuming bacteria that have potential applications in converting methane, a greenhouse gas, to useful fuels and chemicals. How methanotrophs and other bacteria acquire and distribute copper, which is toxic in excess, is not well understood. Here we identify and characterize a previously unknown copper-binding protein implicated in methanotroph copper homeostasis. This protein, MbnP, binds copper with an unusual coordination sphere that includes kynurenine, a tryptophan oxidation product that is produced in vivo by a partner protein, MbnH. MbnP is the founding member of a widespread protein family with potentially broad roles in microbial copper homeostasis.

Copper binding by a unique family of metalloproteins is dependent on kynurenine formation