Oxidation of 1,2,4,5-tetramethoxybenzene by lignin peroxidase of Phanerochaete chrysosporium

Rao S. Koduri, Ross E. Whitwam, David Barr, Steven D. Aust, Ming Tien

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

We have reinvestigated the lignin peroxidase-catalyzed oxidation of 1,2,4,5-tetramethoxybenzene (TMB) by using presteady-state and steady-state kinetic methods. Our presteady-state kinetic results show that the reaction of compound I with TMB obeyed second order kinetics with a rate constant of 1.1 x 107 M-1 s-1. The reaction of compound II with TMB exhibits a hyperbolic concentration dependence with a K(d) of 16 μM and k = 24 s-1. The stoichiometry of TMB oxidation during steady state is two TMB cation radicals formed per H2O2 consumed. These results clearly show that TMB is a good substrate for both compounds I and II of lignin peroxidase.

Original languageEnglish (US)
Pages (from-to)261-265
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume326
Issue number2
DOIs
StatePublished - Feb 15 1996

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Phanerochaete
Oxidation
Kinetics
Stoichiometry
1,2,4,5-tetramethoxybenzene
lignin peroxidase
Cations
Rate constants
Substrates

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Koduri, Rao S. ; Whitwam, Ross E. ; Barr, David ; Aust, Steven D. ; Tien, Ming. / Oxidation of 1,2,4,5-tetramethoxybenzene by lignin peroxidase of Phanerochaete chrysosporium. In: Archives of Biochemistry and Biophysics. 1996 ; Vol. 326, No. 2. pp. 261-265.
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Oxidation of 1,2,4,5-tetramethoxybenzene by lignin peroxidase of Phanerochaete chrysosporium. / Koduri, Rao S.; Whitwam, Ross E.; Barr, David; Aust, Steven D.; Tien, Ming.

In: Archives of Biochemistry and Biophysics, Vol. 326, No. 2, 15.02.1996, p. 261-265.

Research output: Contribution to journalArticle

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AU - Tien, Ming

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AB - We have reinvestigated the lignin peroxidase-catalyzed oxidation of 1,2,4,5-tetramethoxybenzene (TMB) by using presteady-state and steady-state kinetic methods. Our presteady-state kinetic results show that the reaction of compound I with TMB obeyed second order kinetics with a rate constant of 1.1 x 107 M-1 s-1. The reaction of compound II with TMB exhibits a hyperbolic concentration dependence with a K(d) of 16 μM and k = 24 s-1. The stoichiometry of TMB oxidation during steady state is two TMB cation radicals formed per H2O2 consumed. These results clearly show that TMB is a good substrate for both compounds I and II of lignin peroxidase.

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