NDLI: Mössbauer spectroscopic evidence on the heme binding to the proximal histidine in unfolded carbonmonoxy myoglobin by guanidine hydrochloride

Content Provider	Springer Nature Link
Author	Harami, Taikan Kitao, Shinji Kobayashi, Yasuhiro Mitsui, Takaya
Copyright Year	2008
Abstract	The unfolded heme structure in myoglobin is controversial because of no chance of direct X-ray structure analyses. The unfolding of carbonmonoxy myoglobin (MbCO) by guanidine hydrochloride (GdnHCl) was studied by the Mössbauer spectroscopy. The spectra show the presence of a sort of spectrum in the unfolded MbCO, independent on the concentration of GdnHCl from 1 to 6 M and the increase of the fraction of unfolded MbCO, depending on the GdnHCl concentration. The isomer shift of the iron of heme in the unfolded MbCO was identified to be different from that of the native MbCO as the globin structure in Mb collapses under the unfolded conditions. This result and the existing related Mössbauer data proved that the heme in the unfolded MbCO may remain coordinated to the proximal histidine.
Starting Page	179
Ending Page	187
Page Count	9
File Format	PDF
ISSN	03043843
Journal	Hyperfine Interactions
Volume Number	181
Issue Number	1-3
e-ISSN	15729540
Language	English
Publisher	Springer Netherlands
Publisher Date	2008-09-16
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	Carbonmonoxy myoglobin Unfolding Guanidine hydrochloride Mössbauer spectroscopy Isomer shift Surfaces and Interfaces, Thin Films Condensed Matter Atoms, Molecules, Clusters and Plasmas Nuclear Physics, Heavy Ions, Hadrons
Content Type	Text
Resource Type	Article
Subject	Nuclear and High Energy Physics Atomic and Molecular Physics, and Optics Physical and Theoretical Chemistry Condensed Matter Physics

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