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

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Abstract

A comparative study of monomeric soybean and lupin leghemoglobins in the oxy-form was carried out using Mössbauer spectroscopy with a high velocity resolution at 90 K. The 57Fe hyperfine parameters of measured spectra were evaluated and compared with possible structural differences in the heme Fe(II)–O 2 bond.

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Authors and Affiliations

  1. Department of Biochemistry, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India

    A. Kumar

  2. School of Biological Science, 320 Manter Hall, University of Nebraska, Lincoln, NE, 68588, USA

    A. Kumar

  3. Department of Physical Techniques and Devices for Quality Control, Institute of Physics and Technology, Ural Federal University, Ekaterinburg, 620002, Russian Federation

    I. V. Alenkina, M. I. Oshtrakh & V. A. Semionkin

  4. Department of Experimental Physics, Institute of Physics and Technology, Ural Federal University, Ekaterinburg, 620002, Russian Federation

    I. V. Alenkina, A. P. Zakharova, M. I. Oshtrakh & V. A. Semionkin

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  1. A. Kumar
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  2. I. V. Alenkina
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  3. A. P. Zakharova
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  4. M. I. Oshtrakh
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  5. V. A. Semionkin
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Corresponding author

Correspondence to M. I. Oshtrakh.

Additional information

Proceedings of the 5th Joint International Conference on Hyperfine Interactions and International Symposium on Nuclear Quadrupole Interactions (HFI/NQI 2014), Canberra, Australia, 21-26 September 2014

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Kumar, A., Alenkina, I.V., Zakharova, A.P. et al. Hyperfine interactions in soybean and lupin oxy-leghemoglobins studied using Mössbauer spectroscopy with a high velocity resolution. Hyperfine Interact 230, 131–139 (2015). https://doi.org/10.1007/s10751-015-1132-1

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  • DOI: https://doi.org/10.1007/s10751-015-1132-1

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