Article
How periplasmic thioredoxin TlpA reduces bacterial copper chaperone ScoI and cytochrome oxidase subunit II (CoxB) prior to metallation.
The Journal of biological chemistry - 21 Nov 2014
Abicht Helge K, Schärer Martin A, Quade Nick, Ledermann Raphael, Mohorko Elisabeth, Capitani Guido, Hennecke Hauke, Glockshuber Rudi
Abstract excerpt
Two critical cysteine residues in the copper-A site (Cu(A)) on subunit II (CoxB) of bacterial cytochrome c oxidase lie on the periplasmic side of the cytoplasmic membrane. As the periplasm is an oxidizing environment as compared with the reducing cytoplasm, the prediction was that a disulfide bond formed between these cysteines must be eliminated by reduction prior to copper insertion. We show here that a...
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