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DOI:/10.1002/biof.5520140127 79

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560 The structural versatility required to accommodate binding of a broad range of ligands to different sites coupled with the wide distribution of oxidation-sensing Cys residues and low overall sequence similarity among MarR regulators, collectively suggest a model where ligand binding induces a conformational change in the homodimer that cannot be explained by a single sensing site and accompanying pathway of allosteric communication