Heme iron state in various oxyhemoglobins probed using Mossbauer spectroscopy with a high velocity resolution

被引：16
|
作者：
Oshtrakh, M. I. [1 ]
Berkovsky, A. L. [2 ]
Kumar, A. [3 ]
Kundu, S. [3 ]
Vinogradov, A. V. [4 ]
Konstantinova, T. S. [4 ]
Semionkin, V. A. [1 ,5 ]
机构：
[1] Ural Fed Univ, Fac Phys Tech & Devices Qual Control, Ekaterinburg 620002, Russia
[2] Russian Acad Sci, Hematol Res Ctr, Moscow 125167, Russia
[3] Univ Delhi S Campus, Dept Biochem, New Delhi 110021, India
[4] Ural State Med Acad, Ekaterinburg 620028, Russia
[5] Ural Fed Univ, Fac Expt Phys, Ekaterinburg 620002, Russia
来源：
BIOMETALS | 2011年 / 24卷 / 03期
关键词：
Heme iron; Oxyhemoglobins; Mossbauer spectroscopy with a high velocity resolution; Quadrupole splitting; BLOOD-OXYGEN AFFINITY; MOLECULAR-STRUCTURE; HYPERFINE PARAMETERS; ELECTRONIC-STRUCTURE; CONTAINING PROTEINS; MODEL COMPOUNDS; HEMOGLOBIN; SPECTRA; FEATURES; CELLS;
D O I：
10.1007/s10534-011-9428-3
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A comparative study of oxyhemoglobins from pig, rabbit, normal human and patients with blood system malignant diseases was performed using Mossbauer spectroscopy with a high velocity resolution at 90 K. Mossbauer spectra were fitted with the help of two models: using one quadrupole doublet (model of equivalent iron electronic structure in alpha- and beta-subunits of hemoglobins) and superposition of two quadrupole doublets (model of non-equivalent iron electronic structure in alpha- and beta-subunits of hemoglobins). The results obtained using both models demonstrated small variations of hyperfine parameters that were related to the heme iron state variation in different hemoglobins. These results were compared with structural and functional differences of the hemoglobins investigated.
引用
收藏
页码：501 / 512
页数：12
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