On the reactions of lignin peroxidase Compound III (isozyme H8)

Danying Cai, Ming Tien

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

Compound III (oxyperoxidase) of lignin peroxidase isozyme H8 (pI = 3.5) is formed by either reduction of native ferric enzyme (to ferrous) followed by the reaction with dioxygen or by the addition of excess hydrogen peroxide to resting enzyme. When prepared from the ferrous enzyme, Compound III is stable for days. When formed from excess hydrogen peroxide, the enzyme is rapidly inactivated. However, if the hydrogen peroxide is removed by gel filtration, the resulting Compound III exhibits the same stability as when prepared from ferrous enzyme. Compound III of lignin peroxidase is also relatively unreactive to reducing substrates. Addition of veratryl alcohol to Compound III does not result in any reaction. However, when only 1 equivalent of hydrogen peroxide is added to Compound III in the presence of veratryl alcohol, Compound III is converted to resting enzyme and veratraldehyde formation is detected spectroscopically.

Original languageEnglish (US)
Pages (from-to)464-469
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume162
Issue number1
DOIs
StatePublished - Jul 14 1989

Fingerprint

Isoenzymes
Hydrogen Peroxide
Enzymes
Ferrous Compounds
Gel Chromatography
lignin peroxidase
Gels
Oxygen
Substrates
veratryl alcohol

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

@article{db6204df038e4c09a68eed00078b267f,
title = "On the reactions of lignin peroxidase Compound III (isozyme H8)",
abstract = "Compound III (oxyperoxidase) of lignin peroxidase isozyme H8 (pI = 3.5) is formed by either reduction of native ferric enzyme (to ferrous) followed by the reaction with dioxygen or by the addition of excess hydrogen peroxide to resting enzyme. When prepared from the ferrous enzyme, Compound III is stable for days. When formed from excess hydrogen peroxide, the enzyme is rapidly inactivated. However, if the hydrogen peroxide is removed by gel filtration, the resulting Compound III exhibits the same stability as when prepared from ferrous enzyme. Compound III of lignin peroxidase is also relatively unreactive to reducing substrates. Addition of veratryl alcohol to Compound III does not result in any reaction. However, when only 1 equivalent of hydrogen peroxide is added to Compound III in the presence of veratryl alcohol, Compound III is converted to resting enzyme and veratraldehyde formation is detected spectroscopically.",
author = "Danying Cai and Ming Tien",
year = "1989",
month = "7",
day = "14",
doi = "10.1016/0006-291X(89)92020-2",
language = "English (US)",
volume = "162",
pages = "464--469",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

On the reactions of lignin peroxidase Compound III (isozyme H8). / Cai, Danying; Tien, Ming.

In: Biochemical and Biophysical Research Communications, Vol. 162, No. 1, 14.07.1989, p. 464-469.

Research output: Contribution to journalArticle

TY - JOUR

T1 - On the reactions of lignin peroxidase Compound III (isozyme H8)

AU - Cai, Danying

AU - Tien, Ming

PY - 1989/7/14

Y1 - 1989/7/14

N2 - Compound III (oxyperoxidase) of lignin peroxidase isozyme H8 (pI = 3.5) is formed by either reduction of native ferric enzyme (to ferrous) followed by the reaction with dioxygen or by the addition of excess hydrogen peroxide to resting enzyme. When prepared from the ferrous enzyme, Compound III is stable for days. When formed from excess hydrogen peroxide, the enzyme is rapidly inactivated. However, if the hydrogen peroxide is removed by gel filtration, the resulting Compound III exhibits the same stability as when prepared from ferrous enzyme. Compound III of lignin peroxidase is also relatively unreactive to reducing substrates. Addition of veratryl alcohol to Compound III does not result in any reaction. However, when only 1 equivalent of hydrogen peroxide is added to Compound III in the presence of veratryl alcohol, Compound III is converted to resting enzyme and veratraldehyde formation is detected spectroscopically.

AB - Compound III (oxyperoxidase) of lignin peroxidase isozyme H8 (pI = 3.5) is formed by either reduction of native ferric enzyme (to ferrous) followed by the reaction with dioxygen or by the addition of excess hydrogen peroxide to resting enzyme. When prepared from the ferrous enzyme, Compound III is stable for days. When formed from excess hydrogen peroxide, the enzyme is rapidly inactivated. However, if the hydrogen peroxide is removed by gel filtration, the resulting Compound III exhibits the same stability as when prepared from ferrous enzyme. Compound III of lignin peroxidase is also relatively unreactive to reducing substrates. Addition of veratryl alcohol to Compound III does not result in any reaction. However, when only 1 equivalent of hydrogen peroxide is added to Compound III in the presence of veratryl alcohol, Compound III is converted to resting enzyme and veratraldehyde formation is detected spectroscopically.

UR - http://www.scopus.com/inward/record.url?scp=0024344356&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024344356&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(89)92020-2

DO - 10.1016/0006-291X(89)92020-2

M3 - Article

C2 - 2751664

AN - SCOPUS:0024344356

VL - 162

SP - 464

EP - 469

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -