ArticleProceedings of the National Academy of Sciences of the United States of America2026
A redox- and proton-coupled inner membrane transporter mediates copper import to the bacterial cytoplasm.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Copper homeostasis in bacteria requires tightly regulated import systems to balance copper's essential redox functions with its inherent cytotoxicity; yet, the mechanisms of cytoplasmic copper uptake remain poorly understood. In particular, the widespread CopD family of transmembrane proteins has been linked genetically to cytoplasmic copper import, but has not been mechanistically characterized. Here, using in vivo uptake assays, proteoliposome-based, real-time copper translocation kinetic measurements, and spectroscopic and electrochemical analyses, we demonstrate that CopD from the methanotroph
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