Comparison of human oxyhemoglobin in lyophilized form, red blood cells, and concentrated solution: The features of Mössbauer spectra and heme iron stereochemistry / Oshtrakh M.I. // Journal of Inorganic Biochemistry. - 1994. - V. 56, l. 4. - P. 221-231.

ISSN:

01620134

Type:

Article

Abstract:

Mössbauer spectra of human oxyhemoglobin in red blood cells, concentrated solution, and lyophilized form were measured at 87 K. Additionally, Mössbauer spectra of lyophilized oxyhemoglobin were measured at 295 K. The values of quadrupole splitting appeared to be the same for oxyhemoglobin in red blood cells and concentrated solution and slightly lower than those of oxyhemoglobin in lyophilized form. The asymmetry of the Mössbauer absorption line shapes previously observed for oxyhemoglobin in red blood cells was also found for oxyhemoglobin in concentrated solution. These Mössbauer spectra were better fitted using two quadrupole split doublets with almost equal areas. In contrast, Mössbauer spectra of lyophilized oxyhemoglobin were symmetrical and satisfactorily fitted with one quadrupole split doublet. However, these spectra were also fitted with two quadrupole split doublets with equal areas. The variations of the absorption line shapes and parameters of oxyhemoglobin Mössbauer spectra were analyzed in terms of stereochemical differences of the heme iron and Fe(II)O2 bond in α and β-subunits of tetrameric axyhemoglobin. © 1994.

Author keywords:

Index keywords:

ferrous ion; heme; oxyhemoglobin; adult; article; chemical bond; controlled study; erythrocyte; freeze drying; hemoglobin determination; human; human cell; lyophilisate; mossbauer spectroscopy; normal

DOI:

10.1016/0162-0134(94)85102-6

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https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028607610&doi=10.1016%2f0162-0134%2894%2985102-6&partnerID=40&md5=e88ffc7872d8df928762a47e45355be0

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Поле	Значение
Link	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028607610&doi=10.1016%2f0162-0134%2894%2985102-6&partnerID=40&md5=e88ffc7872d8df928762a47e45355be0
Affiliations	Division of Applied Biophysics, Ural State Technical University-UPI1 1 The former Ural Polytechnical Institute., Sverdlovsk, Russian Federation
Chemicals/CAS	ferrous ion, 15438-31-0; heme, 14875-96-8; oxyhemoglobin, 9061-63-6; Heme, 14875-96-8; Iron, 7439-89-6; Macromolecular Systems; Oxyhemoglobins; Solutions
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Correspondence Address	Oshtrakh, M.I.; Division of Applied Biophysics, Ural State Technical University-UPI1 1 The former Ural Polytechnical Institute., Sverdlovsk, Russian Federation
CODEN	JIBID
PubMed ID	7844585
Language of Original Document	English
Abbreviated Source Title	J. Inorg. Biochem.
Source	Scopus