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

Hiroyuki Wariishi, Michael H. Gold

研究成果: ジャーナルへの寄稿記事

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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.

元の言語英語
ページ(範囲)165-168
ページ数4
ジャーナルFEBS Letters
243
発行部数2
DOI
出版物ステータス出版済み - 1 30 1989

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All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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