C0278
Chloroperoxidase from Caldariomyces fumago
buffered aqueous suspension, ≥3,000 units/mL
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Chloride Peroxidase, Chloride:hydrogen-peroxide oxidoreductase
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form
buffered aqueous suspension
Quality Level
mol wt
42 kDa
concentration
≥3,000 units/mL
shipped in
wet ice
storage temp.
2-8°C
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General description
Chloroperoxidase is a heme containing glycoprotein that is secreted from fungus. Chloroperoxidase (CPO) is a extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group.
Application
Chloroperoxidase from Caldariomyces fumagois is useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures. It has been used to study biocatalytic oxidation in polymersome nanoreactors .
It has been used to study biocatalytic oxidation in polymersome nanoreactors.
A useful alternative to lactoperoxidase for 131I ion labeling studies, for bromination of proteins, and for 36Cl labeling of macromolecules in long-term isolation procedures.
Biochem/physiol Actions
Chloroperoxidase (CPO) is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase, catalase and cytochrome P450-type reactions of dehydrogenation, hydrogenperoxide (H2O2) decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs). PAHs are considered to be a potential health risk because of their possible carcinogenic and mutagenic activities and are widely dispersed in the environment.
Unit Definition
One unit will catalyze the conversion of 1.0 μmole of monochlorodimedon to dichlorodimedon per min at pH 2.75 at 25 °C in the presence of potassium chloride and H2O2.
Physical form
Crude suspension in 0.1 M sodium phosphate, pH ~4.5
inhibitor
Product No.
Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Certificates of Analysis (COA)
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The Journal of biological chemistry, 269(19), 13966-13978 (1994-05-13)
Near-ultraviolet resonance Raman spectra of chloroperoxidase derivatives and high valent intermediates show frequencies that can be systematically assigned. In accord with previous observations of low v4 frequencies for the ferric enzyme, and quite low v4 frequencies for the ferrous enzyme
Phytochemistry, 58(6), 929-933 (2001-10-31)
Chloroperoxidase from Caldariomyces fumago was able to chlorinate 17 of 20 aromatic hydrocarbons assayed in the presence of hydrogen peroxide and chloride ions. Reaction rates varied from 0.6 min(-1) for naphthalene to 758 min(-1) for 9-methylanthracene. Mono-, di- and tri-chlorinated
Biophysical journal, 100(4), 1066-1075 (2011-02-16)
Molecular dynamics simulations of an explicitly solvated cis-β-methylstyrene/chloroperoxidase-Compound I complex are performed to determine the cause of the high enantiospecificity of epoxidation. From the simulations, a two-dimensional free energy potential is calculated to distinguish binding potential wells from which reaction
Journal of endodontics, 38(1), 72-74 (2011-12-14)
The aim of this study was to explore the antimicrobial effect of vanadium chloroperoxidase (VCPO) reaction products on Enterococcus faecalis biofilms of 4 different strains. Twenty-four-hour biofilms of E. faecalis strains V583, ER5/1, E2, and OS-16 were incubated in mixtures
Biotechnology letters, 33(10), 1999-2003 (2011-06-11)
The synthesis of halogenated nucleosides and nucleobases is of interest due to their chemical and pharmacological applications. Herein, the enzymatic halogenation of nucleobases and analogues catalysed by microorganisms and by chloroperoxidase from Caldariomyces fumago has been studied. This latter enzyme
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