An analysis of the features of the Mössbauer spectra of soybean leghemoglobin a in oxyand deoxy-forms in relation to protein structure / Kumar A., Zakharova A.P., Alenkina I.V., Oshtrakh M.I., Semionkin V.A. // Bulletin of the Russian Academy of Sciences: Physics. - 2015. - V. 79, l. 8. - P. 1041-1045.

ISSN:
10628738
Type:
Article
Abstract:
An analysis of the Mössbauer spectra of soybean leghemoglobin a in both oxyand deoxy-forms measured with a high velocity resolution at 90 K was carried out in comparison with the room temperature Mössbauer spectrum of the standard absorber sodium nitroprusside. On the basis of the observed features of the spectral line shapes the soybean leghemoglobin a Mössbauer spectra were fitted using two quadrupole doublets for protein oxy-form and three quadrupole doublets for protein deoxy-form. These spectral components were related to two conformational states of His E7 imidazole ring in the distal heme side and three conformational states of His F8 imidazole ring in the proximal heme side for soybean leghemoglobin a oxyand deoxy-forms, respectively. © 2015, Allerton Press, Inc.
Author keywords:
Index keywords:
Porphyrins; Conformational state; High velocity; Protein structures; Quadrupole doublets; Room temperature; Sodium nitroprusside; Spectral components; Spectral line shape; Proteins
DOI:
10.3103/S1062873815080171
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Affiliations Department of Biochemistry, University of Delhi South Campus, New Delhi, India; School of Biological Science, 320 Manter Hall, University of Nebraska, Lincoln, NE, United States; Department of Experimental Physics, Institute of Physics and Technology, Ural Federal University, Ekaterinburg, Russian Federation
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Correspondence Address Oshtrakh, M.I.; Department of Experimental Physics, Institute of Physics and Technology, Ural Federal UniversityRussian Federation
Publisher Allerton Press Incorporation
Language of Original Document English
Abbreviated Source Title Bull. Russ. Acad. Sci. Phys.
Source Scopus