Vanadium chloroperoxidases occur widely in nature

Vollenbroek, Esther G. M.; Simons, Leo; Schijndel, J.W.P.M. van; Barnett, Phil; Balzar, M.; Dekker, Henk; Linden, C. van der; Wever, Ron

doi:10.1042/bst0230267

Cited by 41 publications

(37 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A recent study carried out by our laboratory revealed that the vanadium-type chloroperoxidase appears to be quite widespread, occurring in several different species of hyphomycete fungi (19). Using a probe based upon the active site of CvCPO, it was possible to identify, isolate, and sequence a vanadium chloroperoxidase-encoding gene from the hyphomycete fungus E. didymospora.…”

Section: Discussionmentioning

confidence: 99%

“…We have reported that vanadium chloroperoxidases are present in many other species of terrestrial fungi (19), many of which, including C. inaequalis, are phytopathogens and speculated that in such a case the function of the vanadium chloroperoxidase is to assist in fungal penetration of host cells (20). Here we report the isolation, partial characterization, and gene sequencing of the vanadium chloroperoxidase from the fungus Embellisia didymospora, a species first isolated from the South Adriatic sea (21).…”

mentioning

confidence: 90%

See 1 more Smart Citation

Isolation, Characterization, and Primary Structure of the Vanadium Chloroperoxidase from the Fungus Embellisia didymospora

Barnett

Hemrika

Dekker

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

Here we describe the isolation, purification, and basic kinetic parameters of a vanadium type chloroperoxidase from the hyphomycete fungus Embellisia didymospora. The enzyme proved to possess similar high substrate affinities, a K m of 5 M for a bromide, 1.2 mM for a chloride, and 60 M for a hydrogen peroxide, as those of the vanadium chloroperoxidase from Curvularia inaequalis, although with lower turnover rates for both Cl ؊ and Br ؊ . Substrate bromide was also found to inhibit the enzyme, a feature subsequently also noted for the chloroperoxidase from C. inaequalis. The gene encoding this enzyme was identified using DNA Southern blotting techniques and subsequently isolated and sequenced. A comparison is made between this vanadium chloroperoxidase and that of the fungus C. inaequalis both kinetically and at the sequence level. At the primary structural level the two chloroperoxidases share 68% identity, with conservation of all active site residues.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 90%

Isolation, Characterization, and Primary Structure of the Vanadium Chloroperoxidase from the Fungus Embellisia didymospora

Barnett

Hemrika

Dekker

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…A variety of plant pathogenic ascomycetes that also occur as litter saprophytes have been reported to secrete chloroperoxidases (CPOs) on defined culture media (9,10), and uncharacterized CPO activity has also been detected in soils (11), which generally contain significant fungal biomass (12). Fungal CPOs are hemeor vanadium-containing enzymes that catalyze the H 2 O 2 -dependent oxidation of Cl Ϫ to hypochlorous acid (HOCl) or a similarly reactive chlorine electrophile, and as a result they chlorinate lignin and related aromatic structures in vitro (13-16).…”

mentioning

confidence: 99%

“…They are widely distributed on woody and herbaceous debris in diverse environments, where some of them contribute to lignocellulose breakdown (20). Many members of the order produce haloperoxidase activity on laboratory media (10,21), and in some cases these enzymes have been identified as vanadium CPOs (vCPOs) (22,23). In others, enzymological work has not yet been done, but the presence of DNA sequences with high similarity to known vCPO genes suggests that these enzymes may be produced (e.g., see National Center for Biotechnology Information accession no.…”

mentioning

confidence: 99%

“…EAT82270 for Phaeosphaeria nodorum). Thus, vCPOs could have a major role in global biochlorinations, as first proposed some years ago by Wever and his colleagues (10,23). For our experiments, we selected Curvularia inaequalis, a vCPO-producing, cosmopolitan species in the Pleosporales that has been found on diverse plants, in maritime sand dune soil, and on wood in brackish water (20,(24)(25)(26).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Chlorination of lignin by ubiquitous fungi has a likely role in global organochlorine production

Ortiz-Bermúdez

Hirth

Srebotnik

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Soils and decayed plant litter contain significant quantities of chlorinated aromatic polymers that have a natural but largely unknown origin. We used cupric oxide ligninolysis coupled with gas chromatography/mass spectrometry to show that Curvularia inaequalis, a widely distributed litter ascomycete, chlorinated the aromatic rings of lignin in wood that it was degrading. In aspen wood decayed for 24 weeks, two chlorolignin fragments, 5-chlorovanillin and 2-chlorosyringaldehyde, were each found at Ϸ10 g/g of wood (dry weight). These levels resemble those of similar structures generally found in unpolluted environmental samples. Fractionation of the extractable proteins followed by tandem mass spectrometric analysis showed that the colonized wood contained a previously described C. inaequalis chloroperoxidase that very likely catalyzed lignin chlorination. Chlorolignin produced by this route and humus derived from it are probably significant components of the global chlorine cycle because chloroperoxidase-producing fungi are ubiquitous in decaying lignocellulose and lignin is the earth's most abundant aromatic substance.chloroperoxidase ͉ humus ͉ hypochlorous acid ͉ Pleosporales ͉ soil

show abstract

Vanadium Haloperoxidases

Wever¹,

Hemrika²

2004

Handbook of Metalloproteins

View full text Add to dashboard Cite

This chapter describes the occurrence and the biological function of the vanadium bromoperoxidases and chloroperoxidases. These enzymes that contain vanadate as the prosthetic group catalyze the oxidation of halides to the corresponding hypohalous acids. Purification and molecular characterization of these enzymes is reported and a detailed comparison is made between a bromoperoxidase and a chloroperoxidase, both kinetically as well as structurally. The vanadate‐binding site in haloperoxidases shows an interesting homology with the binding site of phosphate in a large group of phosphatases. Finally, on the basis of mutagenesis studies, a catalytic mechanism is presented for the vanadium chloroperoxidase activity that details the role in catalysis of the amino acid residues in the first coordination sphere of the metal oxide.

show abstract

Vanadium chloroperoxidases occur widely in nature

Cited by 41 publications

References 8 publications

Isolation, Characterization, and Primary Structure of the Vanadium Chloroperoxidase from the Fungus Embellisia didymospora

Isolation, Characterization, and Primary Structure of the Vanadium Chloroperoxidase from the Fungus Embellisia didymospora

Chlorination of lignin by ubiquitous fungi has a likely role in global organochlorine production

Vanadium Haloperoxidases

Contact Info

Product

Resources

About