Bioinorganic Chemistry in Thyroid Gland: Effect of Antithyroid Drugs on Peroxidase-Catalyzed Oxidation and Iodination Reactions

Gouriprasanna, Roy and Mugesh, G (2006) Bioinorganic Chemistry in Thyroid Gland: Effect of Antithyroid Drugs on Peroxidase-Catalyzed Oxidation and Iodination Reactions. In: Bioinorganic Chemistry And Applications . pp. 1-9.

PDF 9.pdf - Published Version Restricted to Registered users only Download (1MB) | Request a copy

Abstract

Propylthiouracil (PTU) and methimazole (MMI) are the most commonly used antithyroid drugs. The available data suggest that these drugs may block the thyroid hormone synthesis by inhibiting the thyroid peroxidase (TPO) or diverting oxidized iodides away from thyroglobulin. It is also known that PTU inhibits the selenocysteine-containing enzyme ID-1 by reacting with the selenenyl iodide intermediate (E-SeI). In view of the current interest in antithyroid drugs, we have recently carried out biomimetic studies to understand the mechanism by which the antithyroid drugs inhibit the thyroid hormone synthesis and found that the replacement of sulfur with selenium in MMI leads to an interesting compound that may reversibly block the thyroid hormone synthesis. Our recent results on the inhibition of lactoperoxidase (LPO)-catalyzed oxidation and iodination reactions by antithyroid drugs are described.

Item Type:	Journal Article
Publication:	Bioinorganic Chemistry And Applications
Publisher:	Hindawi Publishing Corporation
Additional Information:	Copyright of this article belongs to Bioinorganic Chemistry And Applications
Keywords:	Biochemistry & Molecular Biology; Chemistry, Inorganic & Nuclear; Chemistry, Organic;Iodothyronine Deiodinase; Trace-Element Selenium; Hydrogen-Peroxide; Charge-Transfer; Radical Mechanism; Hormone Synthesis; Iodine Complexes; Oxygen-Transfer; Inhibition; Lactoperoxidase
Department/Centre:	Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited:	08 Dec 2008 07:17
Last Modified:	19 Sep 2010 04:54
URI:	http://eprints.iisc.ac.in/id/eprint/16888

Actions (login required)

View Item