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Changes in the Functional Activity of Horseradish Peroxidase and Bovine Serum Albumin in Media with Different Isotope 2H/1H Compositions

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Abstract—It is established that a medium with a reduced content of deuterium has no effect on the secondary structure of horseradish peroxidase and bovine serum albumin and caused no conformational changes in the structures of these proteins. The placement of these proteins in a buffer solution prepared based on deuterium-depleted water led to a decrease in the intensity of intrinsic tryptophan fluorescence, while the circular dichroism spectra remained virtually unchanged. A decrease in the content of deuterium in the reaction medium led to a decrease in the activity of the peroxidase oxidation reaction of o-dianisidine and luminal with hydrogen peroxide.

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Funding

This study was supported by the Russian Foundation for Basic Research (project no. 19-44-233005) and by the state task of Southern Scientific Centre of Russian Academy of Sciences (no. AAAA-A19-119040390083-6).

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Authors and Affiliations

  1. Kuban State University, 350040, Krasnodar, Russia

    S. V. Kozin, A. A. Kravtsov & A. V. Churkina

  2. Southern Scientific Center, Russian Academy of Sciences, 344006, Rostov-on-Don, Russia

    S. V. Kozin, A. A. Kravtsov & V. V. Malyshko

  3. Institute of Cytology, Russian Academy of Sciences, 194064, St. Petersburg, Russia

    K. K. Turoverov, A. V. Fonin & E. V. Chikhirzhina

  4. Kuban State Medical University, Ministry of Health of Russian Federation, 350063, Krasnodar, Russia

    V. V. Malyshko

  5. Kuban State Agrarian University, 350004, Krasnodar, Russia

    A. V. Moiseev

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  1. S. V. Kozin
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  2. A. A. Kravtsov
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Correspondence to S. V. Kozin.

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The authors declare that they have no conflict of interest.This article does not contain any studies involving animals or human participants performed by any of the authors.

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Translated by A. Barkhash

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Kozin, S.V., Kravtsov, A.A., Turoverov, K.K. et al. Changes in the Functional Activity of Horseradish Peroxidase and Bovine Serum Albumin in Media with Different Isotope 2H/1H Compositions. BIOPHYSICS 65, 195–201 (2020). https://doi.org/10.1134/S0006350920020098

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