Caldariomyces

Heme-dependent haloperoxidases generate HOX as reactive species from H2O2 and X, which represents an X+ equivalent capable of undergoing electrophilic addition at electron-rich centers [270,271]. Aprototype biocatalyst of this group is the chloroperoxidase from Caldariomyces Jumago [272]. In many natural systems, such enzymes are responsible for the halogenation of electron-rich aromatic cores. 

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. 

Thus a number of enzymes have been shown to be able to control the oxidation of sulfides to optically active sulfoxides most extensive investigations have concentrated on mono-oxygenases (e.g. from Acinetobacter sp., Pseudomonas putida) and haloperoxidases1 071 (from Caldariomyces fumago and Coral I ina officinalis). A comparison of the methodologies11081 led to the conclusion that the haloperoxidase method was more convenient since the catalysts are more readily available (from enzyme suppliers), the oxidant (H2O2) is cheap and no cofactor recycling is necessary with the haloperoxidases. Typical examples of haloperoxidase-catalysed reactions are described in Scheme 24. 

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... 

Molecular biology chloro-pa oxidase/ Sigma 2000 protein/used isotqjic labeling of maca-mnolecular oanpounds Caldariomyces fumago Woron. (1927), filamentous Eumyc. 

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... 

Despite the enormous versatility and efficiency of CPO in organic synthesis, the natural functions of this enzyme are no less important. In addition to its role in the biosynthesis of caldariomycin and other metabolites (I). CPO is involved in the degradative recycling of humic and fulvic acids (315, 412, 2100, 2108, 2111-2113, 2234, 2235). Both Caldariomyces fumago and Curvularia inaequalis CPO, which... 

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... 

Hashimoto A, Pickard MA (1984) Chloroproxidases from Caldariomyces (= Leptoxyphium) Cultures Glycoproteins with Variable Carbohydrate Content and Isoenzymic Forms. J Gen Microbiol 130 2051... 

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... 

A number of structurally different enzymes have been characterized the heme-thiolate CPO from the marine fungus Caldariomyces fumago (CfCPO), metal-free bacterial CPOs (CPO-L), and vanadium-containing CPOs (VCPOs) from marine algae. 

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