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XAS Study of the Heme Iron Coordination in HIS64(E7)TYR Synthetic Sperm Whale Myoglobin

By using site-directed mutagenesis of the synthetic sperm whale myoglobin, the native distal histidine residue, at position 64 (the helical position E7), was substituted with a tyrosine. The heme iron coordination in wild-type myoglobin and in His(E7)Tyr mutant was studied by X-ray Absorption Spectroscopy (XANES and EXAFS). Data show that the iron is bound to the OH group of tyrosine.