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

  • Deme D
  • Virion A
  • Michot J
 et al. 
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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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Authors

  • D. Deme

  • A. Virion

  • J. L. Michot

  • J. Pommier

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