Hydroxylation of benzene by horseradish peroxidase and immobilized horseradish peroxidase in an organic solvent

Reiko Akasaka, Tadahiko Mashino, Masaaki Hirobe

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Horseradish peroxidase (HRP) catalyzed hydroxylation of benzene with an oxidant when benzene was used as the reaction solvent. HRP immobilized on poly(γ-methyl-L-glutamate) also catalyzed the reaction with higher activity than that of free HRP. The results of the reaction using [18O]hydrogen peroxide show that free and immobilized HRP incorporated the oxygen atom of the reactive species into the product, indicating that both forms of HRP can catalyze hydroxylation of benzene in an analogous manner to that of cytochrome P450.

Original languageEnglish
Pages (from-to)1861-1864
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume5
Issue number16
DOIs
Publication statusPublished - 1995 Aug 17
Externally publishedYes

Fingerprint

Hydroxylation
Horseradish Peroxidase
Benzene
Organic solvents
Oxidants
Cytochrome P-450 Enzyme System
Hydrogen Peroxide
Glutamic Acid
Reactive Oxygen Species
Atoms

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Molecular Biology
  • Molecular Medicine
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

Hydroxylation of benzene by horseradish peroxidase and immobilized horseradish peroxidase in an organic solvent. / Akasaka, Reiko; Mashino, Tadahiko; Hirobe, Masaaki.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 5, No. 16, 17.08.1995, p. 1861-1864.

Research output: Contribution to journalArticle

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