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...
Published in: | Japanese Journal of Applied Physics |
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Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | unknown |
Published: |
IOP Publishing
1993
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Subjects: | |
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 |
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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