Glyoxylate-supported reactions catalyzed by Mn peroxidase of Phanerochaete chrysosporium: Activity in the absence of added hydrogen peroxide

I. Ching Kuan, Ming Tien

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Mn peroxidases are H2O2-utilizing hemeproteins secreted by the lignin-degrading fungus Phanerochaete chrysosporium. We show here that glyoxylate is capable of supporting Mn peroxidase activity without added H2O2. This glyoxylate-supported activity is dependent upon Mn2+ and dioxygen. The involvement of superoxide is demonstrated by inhibition by superoxide scavenging agents, superoxide dismutase, or tetranitromethane. The addition of catalase resulted in dioxygen evolution, indicating that H2O2 is an intermediate in the reaction. Formate is one of the oxidation products of glyoxylate as detected by the formate dehydrogenase assay. The generation of H2O2 in the presence of Mn2+ and Mn peroxidase results in Mn3+ formation. Consequently, we show that the direct reaction between glyoxylate and Mn3+ also results in formate formation. The stoichiometry of this reaction approaches 1:1. Electron spin resonance, spin-trapping studies show formation of the formate radical CO2 in the reaction of Mn3+ and glyoxylate.

Original languageEnglish (US)
Pages (from-to)447-454
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume302
Issue number2
DOIs
StatePublished - Jan 1 1993

Fingerprint

manganese peroxidase
formic acid
Phanerochaete
Hydrogen Peroxide
Superoxides
Tetranitromethane
Formate Dehydrogenases
Oxygen
Hemeproteins
Spin Trapping
Lignin
Scavenging
Electron Spin Resonance Spectroscopy
Fungi
Stoichiometry
Catalase
Superoxide Dismutase
Paramagnetic resonance
Assays
glyoxylic acid

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

@article{6333bcfcfeb3460dafc8808f4be4839b,
title = "Glyoxylate-supported reactions catalyzed by Mn peroxidase of Phanerochaete chrysosporium: Activity in the absence of added hydrogen peroxide",
abstract = "Mn peroxidases are H2O2-utilizing hemeproteins secreted by the lignin-degrading fungus Phanerochaete chrysosporium. We show here that glyoxylate is capable of supporting Mn peroxidase activity without added H2O2. This glyoxylate-supported activity is dependent upon Mn2+ and dioxygen. The involvement of superoxide is demonstrated by inhibition by superoxide scavenging agents, superoxide dismutase, or tetranitromethane. The addition of catalase resulted in dioxygen evolution, indicating that H2O2 is an intermediate in the reaction. Formate is one of the oxidation products of glyoxylate as detected by the formate dehydrogenase assay. The generation of H2O2 in the presence of Mn2+ and Mn peroxidase results in Mn3+ formation. Consequently, we show that the direct reaction between glyoxylate and Mn3+ also results in formate formation. The stoichiometry of this reaction approaches 1:1. Electron spin resonance, spin-trapping studies show formation of the formate radical CO2 in the reaction of Mn3+ and glyoxylate.",
author = "Kuan, {I. Ching} and Ming Tien",
year = "1993",
month = "1",
day = "1",
doi = "10.1006/abbi.1993.1238",
language = "English (US)",
volume = "302",
pages = "447--454",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Glyoxylate-supported reactions catalyzed by Mn peroxidase of Phanerochaete chrysosporium

T2 - Activity in the absence of added hydrogen peroxide

AU - Kuan, I. Ching

AU - Tien, Ming

PY - 1993/1/1

Y1 - 1993/1/1

N2 - Mn peroxidases are H2O2-utilizing hemeproteins secreted by the lignin-degrading fungus Phanerochaete chrysosporium. We show here that glyoxylate is capable of supporting Mn peroxidase activity without added H2O2. This glyoxylate-supported activity is dependent upon Mn2+ and dioxygen. The involvement of superoxide is demonstrated by inhibition by superoxide scavenging agents, superoxide dismutase, or tetranitromethane. The addition of catalase resulted in dioxygen evolution, indicating that H2O2 is an intermediate in the reaction. Formate is one of the oxidation products of glyoxylate as detected by the formate dehydrogenase assay. The generation of H2O2 in the presence of Mn2+ and Mn peroxidase results in Mn3+ formation. Consequently, we show that the direct reaction between glyoxylate and Mn3+ also results in formate formation. The stoichiometry of this reaction approaches 1:1. Electron spin resonance, spin-trapping studies show formation of the formate radical CO2 in the reaction of Mn3+ and glyoxylate.

AB - Mn peroxidases are H2O2-utilizing hemeproteins secreted by the lignin-degrading fungus Phanerochaete chrysosporium. We show here that glyoxylate is capable of supporting Mn peroxidase activity without added H2O2. This glyoxylate-supported activity is dependent upon Mn2+ and dioxygen. The involvement of superoxide is demonstrated by inhibition by superoxide scavenging agents, superoxide dismutase, or tetranitromethane. The addition of catalase resulted in dioxygen evolution, indicating that H2O2 is an intermediate in the reaction. Formate is one of the oxidation products of glyoxylate as detected by the formate dehydrogenase assay. The generation of H2O2 in the presence of Mn2+ and Mn peroxidase results in Mn3+ formation. Consequently, we show that the direct reaction between glyoxylate and Mn3+ also results in formate formation. The stoichiometry of this reaction approaches 1:1. Electron spin resonance, spin-trapping studies show formation of the formate radical CO2 in the reaction of Mn3+ and glyoxylate.

UR - http://www.scopus.com/inward/record.url?scp=0027295913&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027295913&partnerID=8YFLogxK

U2 - 10.1006/abbi.1993.1238

DO - 10.1006/abbi.1993.1238

M3 - Article

C2 - 8387747

AN - SCOPUS:0027295913

VL - 302

SP - 447

EP - 454

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -