HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Chen, Y. P. Articles by Lovell, C. R. Search for Related Content PubMed PubMed Citation Articles by Chen, Y. P. Articles by Lovell, C. R. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 266, Issue 35, 23909-23915, 12, 1991

Purification and properties of a unique flavin-containing chloroperoxidase from the capitellid polychaete Notomastus lobatus

YP Chen, DE Lincoln, SA Woodin and CR Lovell
Department of Biological Sciences, University of South Carolina, Columbia 29208.

A unique flavin-containing chloroperoxidase from the marine worm Notomastus lobatus was purified to homogeneity. This enzyme is composed of two dissociable protein moieties, a flavoprotein and a heme protein, in 1:1 molar ratio. The flavoprotein (Mr = 120,000) consists of four identical subunits having Mr of 30,000, and contains FAD. The heme protein (Mr = 54,000) is composed of two copies each of two non- identical subunits (Mr = 15, 500 and 11, 500) and contains ferriheme. The native N. lobatus chloroperoxidase (Mr = 174,000) therefore has a structure of alpha 4 beta 2 gamma 2. Neither the flavoprotein nor the heme protein alone has detectable chloroperoxidase activity but readily associate to form fully active enzyme. This enzyme is capable of oxidizing Cl-, Br-, and I- with optimum pH values of 4.5, 5.0, and 4.5, respectively, at 440 microM H2O2 and has halide-independent catalase activity in the absence of organic substrate. The enzyme can halogenate a wide variety of aromatic compounds, including phenol, from which it produces 4-bromophenol, 2,4-dibromophenol, and 2,4,6-tribromophenol. The same compounds are found in N. lobatus. The N. lobatus chloroperoxidase is the first haloperoxidase to be purified to homogeneity from a marine polychaete, the first reported to contain flavin, and has several unusual physical and catalytic properties. This chloroperoxidase appears to represent a new class of haloperoxidases.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. R. Kay The Biosynthesis of Differentiation-Inducing Factor, a Chlorinated Signal Molecule Regulating Dictyostelium Development J. Biol. Chem., January 30, 1998; 273(5): 2669 - 2675. [Abstract] [Full Text] [PDF]

				Y. P. Chen, S. A. Woodin, D. E. Lincoln, and C. R. Lovell An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata J. Biol. Chem., March 1, 1996; 271(9): 4609 - 4612. [Abstract] [Full Text] [PDF]