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Exploring the chemistry and biology of vanadium-dependent haloperoxidases - PubMed

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Review

Exploring the chemistry and biology of vanadium-dependent haloperoxidases

Jaclyn M Winter et al. J Biol Chem. 2009.

Abstract

Nature has developed an exquisite array of methods to introduce halogen atoms into organic compounds. Most of these enzymes are oxidative and require either hydrogen peroxide or molecular oxygen as a cosubstrate to generate a reactive halogen atom for catalysis. Vanadium-dependent haloperoxidases contain a vanadate prosthetic group and utilize hydrogen peroxide to oxidize a halide ion into a reactive electrophilic intermediate. These metalloenzymes have a large distribution in nature, where they are present in macroalgae, fungi, and bacteria, but have been exclusively characterized in eukaryotes. In this minireview, we highlight the chemistry and biology of vanadium-dependent haloperoxidases from fungi and marine algae and the emergence of new bacterial members that extend the biological function of these poorly understood halogenating enzymes.

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Figures

FIGURE 1.
FIGURE 1.

Relatedness of V-BrPOs, V-ClPOs, and acid phosphatases identified in fungi, algae, and bacteria and some of their associated chemistry. Phylogenetic analysis was performed using ClustalW (56), and the unrooted neighbor-joining tree was visualized by TreeView. The scale bar indicates 0.1 changes per amino acid. Sequence identification codes include Ci_VClPO from C. inaequalis (accession number CAA59686), hypothetical Rb_VClPO from Rhodopirellula baltica SH1 (CAD72609), Ed_VClPO from E. didymospora (CAA72622), hypothetical Ss1_VClPO from Streptomyces sp. CNQ-525 (ABS50486), hypothetical Ss3_VClPO from Streptomyces sp. CNQ-525 (ABS50491), hypothetical Ss4_VClPO from Streptomyces sp. CNQ-525 (ABS50492), hypothetical Cs_VClPO from Cellulophaga sp. MED134 (ZP_01050453), An_VBrPO from A. nodosum (P81701), Co_VBrPO from C. officinalis (AAM46061), Cp1_VBrPO from C. pilulifera (BAA31261), Cp2_VBrPO from C. pilulifera (BAA31262), hypothetical Sys_VBrPO from Synechococcus sp. CC9311 (YP_731869), Fd_VBrPO from Fucus distichus (AAC35279), Ld1_VBrPO from L. digitata (CAD37191), Ld2_VBrPO from L. digitata (CAD37192), Pi_ACP acid phosphatase from Prevotella intermedia (AB017537), Kp_ACP acid phosphatase from Klebsiella pneumonia (AJ250377), St_ACP acid phosphatase from Salmonella typhimurium (X63599), Ps_ACP acid phosphatase from Providencia stuartii (X64820), and Eb_ACP acid phosphatase from Escherichia blattae (AB020481). Halogenated natural products are α-snyderol (2), β-snyderol (3), γ-snyderol (4), and A80915C (6). Proposed substrates for V-HPOs are (E)-(+)-nerolidol (1) and SF2415B1 (5).

FIGURE 2.
FIGURE 2.

A, vanadium site of native V-ClPO from C. inaequalis. Possible hydrogen bonds are drawn as dashed lines (adapted from Refs. – and 43). B, proposed catalytic scheme of V-ClPO (adapted from Refs. , , and 46).

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References

    1. Butler A., Carter J. N., Simpson M. T. (2001) in Handbook of Metalloproteins (Bertini I., Sigel A., Sigel H. eds) pp. 153–179, Marcel Dekker Inc., New York
    1. Rehder D. (1991) Angew. Chem. Int. Ed. Engl. 30, 148–167
    1. Crans D. C., Smee J. J., Gaidamauskas E., Yang L. (2004) Chem. Rev. 104, 849–902 - PubMed
    1. Littlechild J., Garcia-Rodriguez E., Dalby A., Isupov M. (2002) J. Mol. Recognit. 15, 291–296 - PubMed
    1. Wever R., Hemrika W. (2001) in Handbook of Metalloproteins (Messerschmidt A., Huber R., Wieghardt K., Poulos T. eds) pp. 1417–1428, John Wiley & Sons Ltd., Chichester, United Kingdom

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