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Effect of indole-3-acetic acid on the kinetics of horseradish peroxidase catalyzed scopoletin oxidation

Experientia volume 33, pages 1451–1452 (1977)Cite this article

Summary

The kinetics of horseradish peroxidase catalyzed scopoletin oxidation were observed to be sigmoidal. The apparent Kms for scopoletin is 0.9 mM. Inhibition of scopoletin oxidation by indole-3-acetic acid (IAA) appears to be non competitive. Non competitive inhibition by IAA suggests a more significant role of the peroxidase protein matrix in regulating the activity of the heme moiety.

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Author information

Author notes

  1. Darryel L. Reigh

    Present address: Oklahoma Medical Research Foundation, 825 Northeast 13th Street, 73104, Oklahoma City, Oklahoma., USA

Affiliations

  1. Department of Chemistry, Biochemistry Division, University of Oklahoma, 73069, Norman, Oklahoma, USA

    Darryel L. Reigh & E. C. Smith

Authors
  1. Darryel L. Reigh
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  2. E. C. Smith
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Reigh, D.L., Smith, E.C. Effect of indole-3-acetic acid on the kinetics of horseradish peroxidase catalyzed scopoletin oxidation. Experientia 33, 1451–1452 (1977). https://doi.org/10.1007/BF01918801

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  • DOI: https://doi.org/10.1007/BF01918801

Keywords

  • Oxidation
  • Significant Role
  • Horseradish Peroxidase
  • Protein Matrix
  • Competitive Inhibition