The type I iodothyronine deiodinase (ID-I) in liver and kidney converts the prohormone thyroxine (T4) by outer ring deiodination (ORD) to bioactive 3,3',5-triiodothyronine (T3) or by inner ring deiodination (IRD) to inactive 3,3',5-triiodothronine (rT3), while it also catalyzes the IRD of T3 and the ORD of rT3, with the latter as the preferred substrate. Sulfation of the phenolic hydroxyl group blocks the ORD of T4, while it strongly stimulates the IRD of both T4 and T3, indicating that sulfation is an important step in the irreversible inactivation of thyroid hormone. This review summarizes recent studies concerning this interaction between sulfation and deiodination of iodothyronines, the characterization of iodothyronine sulfotransferase activities, the measurement of iodothyronine sulfates in humans and animals, and the possible physiological importance of iodothyronine sulfation.