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Towards understanding the functioning of a H2O2 sensor


​​​Conventionally, the detection of the intracellular hydrogen peroxide involves the oxidation of a sensor histidine. Exceptionally, PerR, the peroxide sensor encountered in Bacillus subtilis, detects the peroxide via the oxidation of a Fe2+ dependent​ histidine residue. Detailed analyzes of P​erR have always been made complicated by the fact that two separate histidines are succeptibles to be oxidized. The purified protein is then composed of a mixure of non-oxidized, oxidized single and doub​le oxidized forms. After optimizing the obtaining of the oxidized form of PerR at a single histidine, researchers at our institute obtained the first crystal structure of PerR harboring an oxo-histidine.

Published on 20 February 2009

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