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
Even when a small fraction does reach the viable epidermis, the molecule has a short functional half-life unless it is stabilized in the formulation (encapsulation, copper chelation, or both) 1
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The reported Km of glutathione reductase for GSSG is 65 mol /L and for NADPH 8.5 mol /L Erythrocyte lysates were incubated with a saturating concentration of GSSG (1 mmol /L) and either NADPH or NADH (100 mol /L)
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