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 Spectr...

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Bibliographic Details
Published in:Japanese Journal of Applied Physics
Main Authors: Cortes, Robert, Ascone, Isabella, Pin, Serge, Alpert, Bernard, Chiu, Mark L., Sligar, Stephen G.
Format: Article in Journal/Newspaper
Language:unknown
Published: IOP Publishing 1993
Subjects:
Sperm whale
Online Access:http://dx.doi.org/10.7567/jjaps.32s2.544
https://iopscience.iop.org/article/10.7567/JJAPS.32S2.544
https://iopscience.iop.org/article/10.7567/JJAPS.32S2.544/pdf
Description
Summary: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.

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