JBC Origene Your Gene Company

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rodriguez-Lopez, J. N.
Right arrow Articles by Arnao, M. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rodriguez-Lopez, J. N.
Right arrow Articles by Arnao, M. B.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Volume 272, Number 9, Issue of February 28, 1997 pp. 5469-5476
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The Inactivation and Catalytic Pathways of Horseradish Peroxidase with m-Chloroperoxybenzoic Acid
A SPECTROPHOTOMETRIC AND TRANSIENT KINETIC STUDY

(Received for publication, July 30, 1996, and in revised form, October 29, 1996)

Jose Neptuno Rodriguez-Lopez Dagger , Josefa Hernández-Ruiz , Francisco Garcia-Cánovas ** , Roger N. F. Thorneley Dagger , Manuel Acosta and Marino B. Arnao

From the Dagger  Nitrogen Fixation Laboratory, John Innes Centre, NR4 7UH Norwich, United Kingdom and the  Departamento de Biología Vegetal (Fisiología Vegetal) and ** Departamento de Bioquímica y Biología Molecular A, Universidad de Murcia, 30100 Murcia, Spain

The kinetics of the catalytic cycle and irreversible inactivation of horseradish peroxidase C (HRP-C) reacting with m-chloroperoxybenzoic acid (mCPBA) have been studied by conventional and stopped-flow spectrophotometry. mCPBA oxidized HRP-C to compound I with a second order-rate constant k1 = 3.6 × 107 M-1 s-1 at pH 7.0, 25 °C. Excess mCPBA subsequently acted as a one-electron reducing substrate, converting compound I to compound II and compound II to resting, ferric enzyme. In both of these reactions, spectrally distinct, transient forms of the enzyme were observed (lambda max = 411 nm, epsilon  = 45 mM-1 cm-1 for compound I with mCPBA, and lambda max = 408 nm, epsilon  = 77 mM-1 cm-1 for compound II with mCPBA). The compound I-mCPBA intermediate (shown by near infrared spectroscopy to be identical to P965) decayed either to compound II in a catalytic cycle (k3 = 6.4 × 10-3 s-1) or, in a competing inactivation reaction, to verdohemoprotein (ki = 3.3 × 10-3 s-1). Thus, a partition ratio of r = 2 is obtained for the inactivation of ferric HRP-C by mCPBA. The intermediate formed from compound II with mCPBA is not part of the inactivation pathway and only decays via the catalytic cycle to give resting, ferric enzyme (k5 = 1.0 × 10-3 s-1). The data are compared with those from earlier steady-state kinetic studies and demonstrate the importance of single turnover experiments. The results are discussed in terms of the physiologically relevant reactions of plant peroxidases with hydrogen peroxide.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
J. Liu, S. A. Seibold, C. J. Rieke, I. Song, R. I. Cukier, and W. L. Smith
Prostaglandin Endoperoxide H Synthases: PEROXIDASE HYDROPEROXIDE SPECIFICITY AND CYCLOOXYGENASE ACTIVATION
J. Biol. Chem., June 22, 2007; 282(25): 18233 - 18244.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Spolitak, J. H. Dawson, and D. P. Ballou
Reaction of Ferric Cytochrome P450cam with Peracids: KINETIC CHARACTERIZATION OF INTERMEDIATES ON THE REACTION PATHWAY
J. Biol. Chem., May 27, 2005; 280(21): 20300 - 20309.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Yu, S. Girotto, X. Zhao, and R. S. Magliozzo
Rapid Formation of Compound II and a Tyrosyl Radical in the Y229F Mutant of Mycobacterium tuberculosis Catalase-peroxidase Disrupts Catalase but Not Peroxidase Function
J. Biol. Chem., November 7, 2003; 278(45): 44121 - 44127.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Yu, S. Girotto, C. Lee, and R. S. Magliozzo
Reduced Affinity for Isoniazid in the S315T Mutant of Mycobacterium tuberculosis KatG Is a Key Factor in Antibiotic Resistance
J. Biol. Chem., April 18, 2003; 278(17): 14769 - 14775.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. N. P. Hiner, J. H. Ruiz, J. N. R. Lopez, F. G. Canovas, N. C. Brisset, A. T. Smith, M. B. Arnao, and M. Acosta
Reactions of the Class II Peroxidases, Lignin Peroxidase and Arthromyces ramosus Peroxidase, with Hydrogen Peroxide. CATALASE-LIKE ACTIVITY, COMPOUND III FORMATION, AND ENZYME INACTIVATION
J. Biol. Chem., July 19, 2002; 277(30): 26879 - 26885.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. G. Kellner, S.-C. Hung, K. E. Weiss, and S. G. Sligar
Kinetic Characterization of Compound I Formation in the Thermostable Cytochrome P450 CYP119
J. Biol. Chem., March 15, 2002; 277(12): 9641 - 9644.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
G. Wu, C. Wei, R. J. Kulmacz, Y. Osawa, and A.-l. Tsai
A Mechanistic Study of Self-inactivation of the Peroxidase Activity in Prostaglandin H Synthase-1
J. Biol. Chem., April 2, 1999; 274(14): 9231 - 9237.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.