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IZA was purified as a glutathione <jats:italic>S<\/jats:italic>\u2010transferase\u2010fused or His<jats:sub>6<\/jats:sub>\u2010fused protein, and its molecular properties were studied. The UV\u2010visible absorption and EPR spectra of the purified protein showed that IZA bound a heme chromophore in high\u2010spin type. Analysis of the heme indicated that it is of the b\u2003type. Site\u2010directed mutagenesis studies were performed to identify the amino\u2010acid residues that bind the heme to the protein. The results suggest that two Tyr residues, Tyr107 and Tyr113, and a peptide stretch, D99\u2013K102, were important for anchoring the heme into a hydrophobic pocket. The effect of IZA on the steroid 21\u2010hydroxylation reaction was investigated in COS\u20107 cell expression systems. 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