Chloroperoxidase Caldariomyces fumago

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). 

Hernandez, C. E. La Rotta, Lutz, S., Liese, A., and Bon, E. P. S. 2005. Activity and stability of Caldariomyces fumago chloroperoxidase modified by reductive alkila-tion, amidation and cross-linking. Enz Microbial Technol.,37, 582-588. 

Interestingly, it has also been shown that the Caldariomyces fumago chloroperoxidase is able to yield epoxides directly from olefins in the absence of halide... 

Vazquez-Duhalt, R. Ayala, M., and Marquez-Rocha, F. J., Biocatalytic chlorination of aromatic hydrocarbons by chloroperoxidase of Caldariomyces fumago. Phytochemisty, 2001. 58 pp. 929-933. 

Scheme 24 Reactions and conditions i) Chloroperoxidase from Caldariomyces fumago, H2O2, halide ion, H20.

Kaup, B.A., Piantini, U., Wust, M. and Schrader, J., Monoterpenes as novel substrates for oxidation and halo-hydroxylation with chloroperoxidase from Caldariomyces fumago. Appl. Microbiol. Biotechnol., 2007, 73, 1087-1096. 

In the oxidation of aryl methyl sulfides catalyzed by chloroperoxidase from Caldariomyces fumago with racemic 1-phenylethyl hydroperoxide instead of H2O2 as oxygen donor, it was found that (k)-sulfoxides, the (S)-hydroperoxides and the corresponding (k)-alcohol are produced in moderate to good enantiomeric excesses by double stereodifferentiation of the substrate and oxidant (Eq. 2, Table 3) [68]. 

Chloroperoxidase, a fungal en me isolated from Caldariomyces fumago, reacted with 2-methylphenol forming 2-methyl-4-chlorophenol (38% yield) and 2-methyl-6-chlorophenol (Wannstedt et al, 1990). 

Biological. Chloroperoxidase, a fungal enzyme isolated from Caldariomyces fumago, chlorinated 2,4,5-trichlorophenol to give 2,3,4,6-tetrachlorophenol (Wannstedt et al., 1990). 

Several heme-containing proteins, including most peroxidases 12), have been observed to exhibit a low level of catalatic activity, with the chloroperoxidase from Caldariomyces fumago exhibiting the greatest reactivity as a catalase (13-15). Despite the fact that there is as yet only one such example to consider, it provides an alternate mechanism for the catalatic reaction and is addressed in this review. It was first characterized for its ability to chlorinate organic substrates in the presence of chloride and hydrogen peroxide at acid pH, but was later found... 

The ubiquitous hemoprotein chloroperoxidase (CPO) (1) continues to be of great mechanistic and practical interest following its isolation more than 40 years ago from Caldariomyces fumago (2138). The CPO gene from this filamentous fungus has been isolated and sequenced (2139), an active recombinant CPO has been produced (2140), and the crystal structure of this CPO has been determined (2141, 2142). The fungus Curvularia inaequalis contains a vanadium CPO, which has been characterized (primary and X-ray structure) (Fig. 4.1) (2143-2147), as has the vanadium haloperoxidase from Corallina officinalis (2324). This enzyme has also been studied by density functional theory lending support to the proposed mechanism of action (Scheme 4.1) (2325). A related vanadium CPO, which shares 68% primary structural identity with the Curvularia inaequalis CPO, is produced... 

Nuell MJ, Fang G-H, Axley MJ, Kenigsberg P, Hager LP (1988) Isolation and Nucleotide Sequence of the Chloroperoxidase Gene from Caldariomyces fumago. J Bacteriol 170 1007... 

Sundaramoorthy M, Mauro JM, Sullivan AM, Temer J, Poulos TL (1995) Preliminary Crystallographic Analysis of Chloroperoxidase from Caldariomyces fumago. Acta Cryst D51 842... 

Sanfilippo C, Patti A, Nicolosi G (2000) Asymmetric Oxidation of 1,3-Cyclohexadiene Catalysed by Chloroperoxidase from Caldariomyces fumago. Tetrahedron Asym II 3269... 

Vazquez-Duhalt F, Ayala M, Marquez-Rocha FJ (2001) Biocatalytic Chlorination of Aromatic Hydrocarbons by Chloroperoxidase of Caldariomyces fumago. Phytochemistry 58 929... 

Chloroperoxidase derived from the microorganism Caldariomyces fumago combined with sodium chloride and hydrogen peroxide in buffered aqueous solution converts olefins to chlorohydrines374"376. Chloroperoxidase immobilized on a polymeric support catalyzes the bromination of barbituric acid in a continuous flow system377. Detailed mechanistic study on the mono- and dibromination of barbituric acid catalyzed by bromoperoxidase from Ascophyllum nodosum has been reported by Franssen and coworkers378. Pyrimidine bases are chlorinated and brominated by chloroperoxidase379. 

Fig. 5.19 Three oxygen transfer reactions catalyzed by the chloroperoxidase from Caldariomyces fumago in which the oxygen transfer was firmly established by [lsO] isotopic labeling studies...

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