Thyroid hormone synthesis and thyroglobulin iodination related to the peroxidase localization of oxidizing equivalents: Studies with cytochrome c peroxidase and horseradish peroxidase

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Abstract

Cytochrome c peroxidase (CcP) and horseradish peroxidase (HRP), when combined with a stoichiometric amount of H2O2, form stable compounds I which are known as FeIV R{ring operator} and FeIV \ ̊gp+structures, respectively. These compounds were assayed in the catalysis of thyroid hormone synthesis and the iodination reaction. As previously shown for the lactoperoxidase FeIV R{ring operator} compound, the CcP FeIV R{ring operator} compound was involved in the coupling and not in the iodination reactions. In contrast, the HRP FeIV \ ̊gp+compound catalyzed both iodination and hormone formation. The possible role of the different peroxidase-H2O2compounds in the two sequential reactions, thyroglobulin iodination and thyroid hormone formation, is discussed. © 1985.

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Deme, D., Virion, A., Michot, J. L., & Pommier, J. (1985). Thyroid hormone synthesis and thyroglobulin iodination related to the peroxidase localization of oxidizing equivalents: Studies with cytochrome c peroxidase and horseradish peroxidase. Archives of Biochemistry and Biophysics, 236(2), 559–566. https://doi.org/10.1016/0003-9861(85)90659-9

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