Lignin peroxidase compound III. Formation, inactivation, and conversion to the native enzyme

Hiroyuki Wariishi, Michael H. Gold

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

At pH 3.0 in the absence of a reducing substrate and the presence of only 20 equivalents of H2O2, lignin peroxidase (LiP) is readily converted to LiP compound III (LiPIII) (Fe(III)O- 2 - complex). LiPIII which is produced via the reaction of LiP compound II (LiPII) with H2O2 is not part of the peroxidase catalytic cycle, and is readily and irreversibly inactivated. Veratryl alcohol (VA), a Phanerochaete chrysosporium secondary metabolite, protects the enzyme from inactivation via two mechanisms. Acting as a substrate, VA reduces LiPII to regenerate the native enzyme. Secondly, the binding of VA to LiPIII rapidly displaces O.- 2/HO.- 2, thereby converting LiPIII directly to the native enzyme. VA is not consumed during this displacement reaction. These results help to explain the role of VA in stabilizing the enzyme in the presence of excess H2O2.

Original languageEnglish
Pages (from-to)165-168
Number of pages4
JournalFEBS Letters
Volume243
Issue number2
DOIs
Publication statusPublished - Jan 30 1989
Externally publishedYes

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Enzymes
Phanerochaete
Substrates
Metabolites
Peroxidase
veratryl alcohol
lignin peroxidase

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Lignin peroxidase compound III. Formation, inactivation, and conversion to the native enzyme. / Wariishi, Hiroyuki; Gold, Michael H.

In: FEBS Letters, Vol. 243, No. 2, 30.01.1989, p. 165-168.

Research output: Contribution to journalArticle

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