Chloroperoxidase properties

Chen YP, DE Lincol, SA Woodin, CR Lovell (1991) Purification and properties of a unique flavin-containing chloroperoxidase from the capitellid polychaete Notomastus lobatus. J Biol Chem 266 23909-23915. 

Morris DR, LP Hager (1966) Chloroperoxidase 1 Isolation and properties of the crystalline protein. J Biol Chem 241 1763-1768. 

Morris DR, Hager LP (1966) Chloroperoxidase I. Isolation and Properties of the Crystalline Glycoprotein. J Biol Chem 241 1763... 

Burd W, Yourkevich O, Voskoboev AJ, van Pee K-H (1995) Purification and Properties of a Non-Haem Chloroperoxidase from Serratia marcescens. FEMS Microbiol Lett 129 255... 

Petri A, Gambicorti T, Salvadori P (2004) Covalent Immobilization of Chloroperoxidase on Silica Gel and Properties of the Immobilized Biocatalyst. J Mol Catal B Enzym 27 103... 

In addition to plant and animal sources, peroxidases are also found in mould, bacteria and microorganisms. A peroxidase from the mould Caldariomyces fumago, chloroperoxidase, has been isolated and characterised. Like the plant peroxidases it has ferriprotoporphyrin IX as the prosthetic group. In many of its chemical and physical properties chloroperoxidase is similar to horseradish peroxidase, but it has the unique ability amongst peroxidases to catalyse the oxidation of chloride ion (Hager et al., 1966 Morris and Hager, 1966). 

Horseradish peroxidase (HRP) is a hemeprotein which catalyses the oxidation of a large variety of inorganic and organic substrates (Dunford and Stillman, 1976). Chloroperoxidase (CPO) is a versatile heme enzyme since it shares similar properties with classical peroxidases and P-450 monooxygenases and also catalyses the oxidative halogenation of organic substrates (Blake and Hager, 1990). 

Borowski, T., Szczepanik, W., Chruszcz, M. and Broclawik, E. (2004). First principle calculations for the active centres in vanadium-containing chloroperoxidase and its functional models geometrical and spectral properties. International Journal of Quantum Chemistry, 99,864-875. 

Fig. 6.10 Schematic representation of the protein modification approaches applied to four peroxidases (Horseradish, chloroperoxidase, cytochrome c, and C. cinereous peroxidase) and proteins with pseudoperoxidase activity (cytochrome P450, myoglobin, and cytochrome c). The dashed arrows link each specific protein modification with the properties improved...

Aburto J, Ayala M, Bustos-Jaimes I et al (2005) Stability and catalytic properties of chloroperoxidase immobilized on SBA-16 mesoporous materials. Microporous Mesoporous Mater 83 193-200... 

Jung D, Paradiso M, Wallacher D et al (2009) Formation of cross-linked chloroperoxidase aggregates in the pores of mesocellular foams characterization by SANS and catalytic properties. ChemSusChem 2 161-164... 

Aoun S, Chebli C, Baboulene M (1998) Noncovalent immobilization of chloroperoxidase onto talc catalytic properties of a new biocatalyst. Enzyme Microb Technol 23 380-385... 

Ueno, T., Kousumi, Y., Yoshizawa-Kumagaye, K., Nakajima, K., Ueyama, N., Okamura, T., and Nakamura, N. (2001) Role of a-Helix Conformation Cooperating with NH—S Hydrogen Bond in the Active Site of Cytochrome P-450 and Chloroperoxidase Synthesis and Properties of [MIII(OEP)(Cys-Helical Peptide)] (M = Fe and Ga), J. Am. Chem. Soc. 120, 12264-12273. 

Asplund G., Christiansen J. V., and Grimvall A. (1993) A chloroperoxidase-like catalyst in soil detection and characterization of some properties. Soil Biol. Biochem. 25, 41 -46. 

Choline dihydrogenphosphate, choline acetate and choline citrate (Scheme 4) show improved properties, with respect common molecular solvents and imidazolium based ILs, also in the chloroperoxidase-catalyzed reactions." In the presence of these cosolvents (up to 70%) the conversion of methyl phenyl sulfide to the corresponding sulfoxide, leads to satisfactory yields and very good enantioselectivities. In addition, over-oxidation of the sulfoxide to the sulfone is not observed. 

Preparation and properties of ferrous chloroperoxidase complexes with dioxygen, nitric-oxide, and an alkyl isocyanide—spectroscopic dissimilarities between the oxygenated forms of chloroperoxidase and cytochrome-P-450. J. Biol. Chem. 260, 5530-5535. 

Pahna C, Moreira MT, Feijoo G et al. (1997) Enhanced catalytic properties of MnP by exogenous addition of manganese and hydrogen peroxide. Biotechnol Lett 19(3) 263—267 Pasta P, Carrea G, Monzani E et til. (1999). Chloroperoxidase-catalyzed enantioselective oxidation of methyl phenyl sulfide with dihydroxyfumaric add/oxygen or ascorbic acid/oxygen as oxidants. Biotechnol Bioeng 62(4) 489-493... 

Cytochrome P-450 and chloroperoxidase have catalytic and spectral properties that differ significantly from those of other heme systems. As the current state of knowledge of these two proteins has been extensively reviewed [20-29], we focus here on the structural origin of their unique spectral properties and the correlation of these properties with the novel catalytic activities of the enzymes. As will be shown, both enzymes are now well established to be thiolate-ligated heme systems. 

The absorption spectrum of the Compound I form of chloroperoxidase is different from that of horseradish peroxidase Compound I, and is more closely analogous to that of catalase Compound I. This suggests that it may also have a Aiu ground state [22, 50]. However, the EPR spectrum of chloroperoxidase Compound I indicates that there is electron density at the meso carbons this finding is inconsistent with a Ai ground electronic state [50, 93]. Thus, the different absorption spectral properties of the Compound I intermediates of peroxidases may not derive solely from differences in orbital symmetry. Rather, other factors such as the nature of the axial ligand or the macrocycle stereochemistry may be responsible for these spectral differences. 

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