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Effect of Mn2+, Co2+, Ni2+, and Cu2+ on horseradish peroxidase

Activation, inhibition, and denaturation studies

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Abstract

The effects of transition metal ions (M2+) such as Mn2+, Co2+, Ni2+, and Cu2+ on the functional and structural stabilities of horseradish peroxidase (HRP) were investigated with respect to reversible chemical denaturation, Michaelis-Menten kinetics, chemical modification and time-dependent catalytic activity. Conformational Gibbs free energy (ΔG°(H2O)) as a structural stability criterion and transition concentrations of metal ions ([M2+]1/2) were estimated using a two-state chemical denaturation model. Activation and inhibitory concentration ranges for each metal ion were specified by the steady-state enzyme kinetics. Results of a pH-profile method confirmed by chemical modification indicate that a histidine residue interacts in the activation concentration range, whereas carboxylic residues (Asp and Glu) contribute to interaction in the inhibitory concentration range. Incubation of the enzyme with the metal ion at activation concentration leads to long-term functional stability of peroxidase. Thus, such metal ions as potent effectors induced the enhancement of conformational and functional stabilities of horseradish peroxidase.

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Authors and Affiliations

  1. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    A. Mahmoudi & A. A. Moosavi-Movahedi

  2. Chemistry Department, Tehran Northern Branch, Islamic Azad University, Tehran, Iran

    A. Mahmoudi & N. Mohammadian

  3. Inhibitors Department, Research Institute of Petroleum Industry, N.I.O.C., Tehran, Iran

    K. Nazari

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  1. A. Mahmoudi
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  2. K. Nazari
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  3. N. Mohammadian
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  4. A. A. Moosavi-Movahedi
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Correspondence to A. A. Moosavi-Movahedi.

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Mahmoudi, A., Nazari, K., Mohammadian, N. et al. Effect of Mn2+, Co2+, Ni2+, and Cu2+ on horseradish peroxidase. Appl Biochem Biotechnol 104, 81–94 (2003). https://doi.org/10.1385/ABAB:104:1:81

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  • DOI: https://doi.org/10.1385/ABAB:104:1:81

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