Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871147 | FEBS Letters | 2012 | 6 Pages |
Abstract
⺠Protein-disulfide reductases are important in the oxidizing environment of the bacterial periplasm for keeping target proteins with vicinal cysteine residues in the reduced, dithiol state. ⺠The Bradyrhizobium japonicum TlpA protein is reported here to reduce the oxidized form of ScoI, a widespread copper-binding chaperone. ⺠By reducing ScoI, the TlpA protein prepares this target protein for the binding of copper, thus ensuring that the metal can subsequently become inserted into heme-copper cytochrome oxidases.
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Authors
Elisabeth Mohorko, Helge K. Abicht, Doris Bühler, Rudi Glockshuber, Hauke Hennecke, Hans-Martin Fischer,