Abstract
Previous studies on the peroxidase-catalyzed iodination of tyrosine have been complicated by non-enzymatic reactions between iodine and tyrosine. The low pH optimum for chloroperoxidase allowed tyrosine iodination to be studied without this complication. Chloroperoxidase catalyzes the iodination reaction in two distinct stages. First, iodide ion is peroxidized to form molecular iodine. Secondly, the enzyme catalyzes a reaction between iodine, hydrogen peroxide, and tyrosine. This second reaction has an absolute requirement for hydrogen peroxide, and is inhibited by the presence of iodide ion.
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