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Peroxidase Activity of Leghemoglobin of Bean (Vicia faba L.) Nodules in Relation to Tert-Butyl Hydroperoxide

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Abstract

Like many other hemoglobins, leghemoglobin (Lb), the hemoglobin of legume nodules, demonstrates peroxidase activity and can oxidize various substances with the participation of H2O2 or organic peroxides. The peroxidase activity of Lb isolated from bean nodules (Vicia faba L.) was studied in reaction with tert-butyl hydroperoxide, an analog of organic hydroperoxides, and o-dianisidine as a reducing substrate. The reaction catalyzed by Lb had classical Michaelis kinetics (Vmax = 1.3 M/min ⋅ mM of heme, Km = 0.8 mmol/L). The substrate concentrations that do not limit the peroxidase reaction rate were determined: 0.8 mmol/L for o-dianisidine and 1 mmol/L for tert-butyl hydroperoxide. With a pH decrease from 9 to 6, the Lb peroxidase activity increased by almost two times. This may be important for nodules in vivo, for example, during their aging, when the pH decreases and the oxidized Lb content increases. Although Lb is inferior in peroxidase activity to the true peroxidases, it can provide additional antioxidant protection under oxidative stress due to its high concentration in nodules.

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ACKNOWLEDGMENTS

The research was carried out on the equipment of the Shared-Access Equipment Center of Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences.

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  1. Bach Institute of Biochemistry, Federal Research Center Fundamentals of Biotechnology, Russian Academy of Sciences, 119071, Moscow, Russia

    O. V. Kosmachevskaya, E. I. Nasybullina & A. F. Topunov

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Kosmachevskaya, O.V., Nasybullina, E.I. & Topunov, A.F. Peroxidase Activity of Leghemoglobin of Bean (Vicia faba L.) Nodules in Relation to Tert-Butyl Hydroperoxide. Appl Biochem Microbiol 58, 37–44 (2022). https://doi.org/10.1134/S0003683822010045

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