57Fe quadrupole splitting and isomer shift in various oxyhemoglobins: study using Mössbauer spectroscopy

Author: Oshtrakh M.   Berkovsky A.   Kumar A.   Kundu S.   Vinogradov A.   Konstantinova T.   Semionkin V.  

Publisher: Springer Publishing Company

ISSN: 0304-3843

Source: Hyperfine Interactions, Vol.197, Iss.1-3, 2010-04, pp. : 301-307

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Abstract

A comparative study of normal human, rabbit and pig oxyhemoglobins and oxyhemoglobin from patients with chronic myeloleukemia and multiple myeloma using Mössbauer spectroscopy with a high velocity resolution demonstrated small variations of the 57Fe quadrupole splitting and isomer shift. These variations may be a result of small structural differences in the heme iron stereochemistry of various hemoglobins.