Oxidation of guaiacol by lignin peroxidase: Role of veratryl alcohol

R. S. Koduri, Ming Tien

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

We have investigated the lignin peroxidase-catalyzed oxidation of guaiacol and the role of veratryl alcohol in this reaction by steady-state and pre- steady-state methods. Pre-steady-state kinetic analyses demonstrated that guaiacol is a good substrate for both compounds I and II, the two- and one- electron oxidized enzyme intermediates, respectively, of lignin peroxidase. The rate constant for the reaction with compound I is 1.2 x 106 M-1 s- 1. The reaction of guaiacol with compound II exhibits a K(d) of 64 μM and a first-order rate constant of 17 s-1. Oxidation of guaiacol leads to tetraguaiacol formation. This reaction exhibits classical Michaelis-Menten kinetics with a K(m) of 160 μM and a k(cat) of 7.7 s-1. Veratryl alcohol, a secondary metabolite of ligninolytic fungi, is capable of mediating the oxidation of guaiacol. This was shown by steady-state inhibition studies. Guaiacol completely inhibited the oxidation of veratryl alcohol, whereas veratryl alcohol had no corresponding inhibitory effect on guaiacol oxidation. In fact, at low guaiacol concentrations, veratryl alcohol stimulated the rate of guaiacol oxidation. These results collectively demonstrate that veratryl alcohol can serve as a mediator for phenolic substrates in the lignin peroxidase reaction.

Original languageEnglish (US)
Pages (from-to)22254-22258
Number of pages5
JournalJournal of Biological Chemistry
Volume270
Issue number38
DOIs
StatePublished - Jan 1 1995

Fingerprint

Guaiacol
Oxidation
Rate constants
veratryl alcohol
lignin peroxidase
guaiacol peroxidase
Kinetics
Substrates
Metabolites
Fungi
Electrons

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{b1361ad31373434792b6da6ef2c06744,
title = "Oxidation of guaiacol by lignin peroxidase: Role of veratryl alcohol",
abstract = "We have investigated the lignin peroxidase-catalyzed oxidation of guaiacol and the role of veratryl alcohol in this reaction by steady-state and pre- steady-state methods. Pre-steady-state kinetic analyses demonstrated that guaiacol is a good substrate for both compounds I and II, the two- and one- electron oxidized enzyme intermediates, respectively, of lignin peroxidase. The rate constant for the reaction with compound I is 1.2 x 106 M-1 s- 1. The reaction of guaiacol with compound II exhibits a K(d) of 64 μM and a first-order rate constant of 17 s-1. Oxidation of guaiacol leads to tetraguaiacol formation. This reaction exhibits classical Michaelis-Menten kinetics with a K(m) of 160 μM and a k(cat) of 7.7 s-1. Veratryl alcohol, a secondary metabolite of ligninolytic fungi, is capable of mediating the oxidation of guaiacol. This was shown by steady-state inhibition studies. Guaiacol completely inhibited the oxidation of veratryl alcohol, whereas veratryl alcohol had no corresponding inhibitory effect on guaiacol oxidation. In fact, at low guaiacol concentrations, veratryl alcohol stimulated the rate of guaiacol oxidation. These results collectively demonstrate that veratryl alcohol can serve as a mediator for phenolic substrates in the lignin peroxidase reaction.",
author = "Koduri, {R. S.} and Ming Tien",
year = "1995",
month = "1",
day = "1",
doi = "10.1074/jbc.270.38.22254",
language = "English (US)",
volume = "270",
pages = "22254--22258",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "38",

}

Oxidation of guaiacol by lignin peroxidase : Role of veratryl alcohol. / Koduri, R. S.; Tien, Ming.

In: Journal of Biological Chemistry, Vol. 270, No. 38, 01.01.1995, p. 22254-22258.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Oxidation of guaiacol by lignin peroxidase

T2 - Role of veratryl alcohol

AU - Koduri, R. S.

AU - Tien, Ming

PY - 1995/1/1

Y1 - 1995/1/1

N2 - We have investigated the lignin peroxidase-catalyzed oxidation of guaiacol and the role of veratryl alcohol in this reaction by steady-state and pre- steady-state methods. Pre-steady-state kinetic analyses demonstrated that guaiacol is a good substrate for both compounds I and II, the two- and one- electron oxidized enzyme intermediates, respectively, of lignin peroxidase. The rate constant for the reaction with compound I is 1.2 x 106 M-1 s- 1. The reaction of guaiacol with compound II exhibits a K(d) of 64 μM and a first-order rate constant of 17 s-1. Oxidation of guaiacol leads to tetraguaiacol formation. This reaction exhibits classical Michaelis-Menten kinetics with a K(m) of 160 μM and a k(cat) of 7.7 s-1. Veratryl alcohol, a secondary metabolite of ligninolytic fungi, is capable of mediating the oxidation of guaiacol. This was shown by steady-state inhibition studies. Guaiacol completely inhibited the oxidation of veratryl alcohol, whereas veratryl alcohol had no corresponding inhibitory effect on guaiacol oxidation. In fact, at low guaiacol concentrations, veratryl alcohol stimulated the rate of guaiacol oxidation. These results collectively demonstrate that veratryl alcohol can serve as a mediator for phenolic substrates in the lignin peroxidase reaction.

AB - We have investigated the lignin peroxidase-catalyzed oxidation of guaiacol and the role of veratryl alcohol in this reaction by steady-state and pre- steady-state methods. Pre-steady-state kinetic analyses demonstrated that guaiacol is a good substrate for both compounds I and II, the two- and one- electron oxidized enzyme intermediates, respectively, of lignin peroxidase. The rate constant for the reaction with compound I is 1.2 x 106 M-1 s- 1. The reaction of guaiacol with compound II exhibits a K(d) of 64 μM and a first-order rate constant of 17 s-1. Oxidation of guaiacol leads to tetraguaiacol formation. This reaction exhibits classical Michaelis-Menten kinetics with a K(m) of 160 μM and a k(cat) of 7.7 s-1. Veratryl alcohol, a secondary metabolite of ligninolytic fungi, is capable of mediating the oxidation of guaiacol. This was shown by steady-state inhibition studies. Guaiacol completely inhibited the oxidation of veratryl alcohol, whereas veratryl alcohol had no corresponding inhibitory effect on guaiacol oxidation. In fact, at low guaiacol concentrations, veratryl alcohol stimulated the rate of guaiacol oxidation. These results collectively demonstrate that veratryl alcohol can serve as a mediator for phenolic substrates in the lignin peroxidase reaction.

UR - http://www.scopus.com/inward/record.url?scp=0029160709&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029160709&partnerID=8YFLogxK

U2 - 10.1074/jbc.270.38.22254

DO - 10.1074/jbc.270.38.22254

M3 - Article

C2 - 7673205

AN - SCOPUS:0029160709

VL - 270

SP - 22254

EP - 22258

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 38

ER -