Study of human, rabbit and pig oxyhemoglobins using high velocity resolution Mossbauer spectroscopy in relation to their structural and functional variations

被引：13
|
作者：
Oshtrakh, M. I. [1 ]
Kumar, A. [4 ]
Kundu, S. [4 ]
Berkovsky, A. L. [3 ]
Semionkin, V. A. [1 ,2 ]
机构：
[1] Ural Fed Univ, Fac Phys Tech & Devices Qual Control, Ekaterinburg 620002, Russia
[2] Ural Fed Univ, Fac Expt Phys, Ekaterinburg 620002, Russia
[3] Russian Acad Med Sci, Hematol Res Ctr, Moscow 125167, Russia
[4] Univ Delhi S Campus, Dept Biochem, New Delhi 110021, India
来源：
JOURNAL OF MOLECULAR STRUCTURE | 2011年 / 993卷 / 1-3期
关键词：
Human adult; rabbit and pig oxyhemoglobins; Mossbauer spectroscopy with a high velocity resolution; Hyperfine parameters; Heme iron structure; BLOOD-OXYGEN AFFINITY; BIOMEDICAL-RESEARCH; HEMOGLOBIN; STEREOCHEMISTRY; FEATURES; SPECTRA; CELLS;
D O I：
10.1016/j.molstruc.2010.11.035
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
Normal human adult, rabbit and pig oxyhemoglobins in frozen red blood cell solutions were studied using Mossbauer spectroscopy with a high velocity resolution. Spectra were analyzed using two models with and without accounting for the heme iron electronic structure non-equivalence in alpha- and beta-subunits of tetrameric hemoglobins. The observed differences of Mossbauer hyperfine parameters were related to structural variations in human, rabbit and pig oxyhemoglobins as well as to the differences in ligand binding affinities of these proteins. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码：292 / 296
页数：5
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