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- W2892120954 endingPage "113" @default.
- W2892120954 startingPage "101" @default.
- W2892120954 abstract "In the last two decades, there has been great advance in the understanding of bacterial copper homeostasis and toxicity mechanisms. A minimum of three proteins form the core of copper homeostasis in all bacteria: A copper-exporting ATPase that pumps copper across the cytoplasmic membrane, a copper chaperone, which sequesters and routes cytoplasmic copper, and a copper-responsive regulator that regulates the expression of these proteins. Gram-negative organisms possess additional components, such as copper export systems to traverse the outer membrane, periplasmic multicopper oxidases, and periplasmic copper chaperones. Recent work has also changed the understanding of copper toxicity. Rather than oxidative damage, copper’s main toxic effect appears to lie in its ability to displace iron from iron–sulfur cluster proteins, thereby inactivating key enzymes. However, how cuproenzymes are metallated and how copper enters the bacterial cytoplasm is still poorly understood." @default.
- W2892120954 created "2018-09-27" @default.
- W2892120954 creator A5073996154 @default.
- W2892120954 date "2019-01-01" @default.
- W2892120954 modified "2023-10-16" @default.
- W2892120954 title "Copper Disposition in Bacteria" @default.
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