Hyperfine interactions in soybean and lupin oxy-leghemoglobins studied using Mossbauer spectroscopy with a high velocity resolution

被引:2
|
作者
Kumar, A. [1 ,2 ]
Alenkina, I. V. [3 ,4 ]
Zakharova, A. P. [4 ]
Oshtrakh, M. I. [3 ,4 ]
Semionkin, V. A. [3 ,4 ]
机构
[1] Univ Delhi, Dept Biochem, New Delhi 110021, India
[2] Univ Nebraska, Sch Biol Sci, Lincoln, NE 68588 USA
[3] Ural Fed Univ, Inst Phys & Technol, Dept Phys Tech & Devices Qual Control, Ekaterinburg 620002, Russia
[4] Ural Fed Univ, Inst Phys & Technol, Dept Expt Phys, Ekaterinburg 620002, Russia
来源
HYPERFINE INTERACTIONS | 2015年 / 231卷 / 1-3期
关键词
Mossbauer spectroscopy; Soybean and lupin oxy-leghemoglobins; Heme iron stereochemistry; Hyperfine interactions; HEME IRON STEREOCHEMISTRY; CONTAINING PROTEINS; BIOMEDICAL-RESEARCH; HUMAN OXYHEMOGLOBIN; SPECTRA; FEATURES; HEMOGLOBIN; STATE;
D O I
10.1007/s10751-015-1132-1
中图分类号
O64 [物理化学(理论化学)、化学物理学]; O56 [分子物理学、原子物理学];
学科分类号
070203 ; 070304 ; 081704 ; 1406 ;
摘要
A comparative study of monomeric soybean and lupin leghemoglobins in the oxy-form was carried out using Mossbauer spectroscopy with a high velocity resolution at 90 K. The Fe-57 hyperfine parameters of measured spectra were evaluated and compared with possible structural differences in the heme Fe(II)-O (2) bond.
引用
收藏
页码:131 / 139
页数:9
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