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Function
Haloperoxidases catalyze the oxidation of halides by hydrogen peroxide while adding a halide to hydrocarbons. They are classified as chloroperoxldase (CPO), bromoperoxidase (BPO) and iodoperoxidase (IPO) according to the halide which they oxidize.
- CPO is heme-containing, vanadium-containing or metal-free.
- BPO is from marine algae is vanadium-containing[1].
Structural highlights
The vanadate ion shows a trigonal bipyramidal coordination. The iodine atoms are coordinated to tyrosine residues: first coordination site and second coordination site [2]. Water molecules shown as red spheres.
- ↑ Winter JM, Moore BS. Exploring the chemistry and biology of vanadium-dependent haloperoxidases. J Biol Chem. 2009 Jul 10;284(28):18577-81. doi: 10.1074/jbc.R109.001602. Epub, 2009 Apr 10. PMID:19363038 doi:https://dx.doi.org/10.1074/jbc.R109.001602
- ↑ Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D. X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution. J Mol Biol. 1999 Oct 29;293(3):595-611. PMID:10543953 doi:10.1006/jmbi.1999.3179
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3D structures of haloperoxidase
Updated on 07-August-2025
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- Vanadium-dependent chloroperoxidase
- Heme-containing chloroperoxidase
- Metal-free chloroperoxidase
- 1a7u - SaCPO T – Streptomyces aureofaciens
- 1a8s – PfCPO F + propanoic acid – Pseudomonas fluorescens
- 1a8u – PfCPO T + benzoic acid
- 1a88 - CPO L – Streptomyces lividans
- 4dgq – CPO – Burkholderia cenocepacia
- Metal-free bromoperoxidase
- Vanadium-containing bromoperoxidase
- 1qi9 – AnBPO + I + VO4 – Ascophyllum nodosum
- 5aa6 – AnBPO-2 + VO4
- 1up8, 1qhb, 7qyy – CpBPO – Corallina pilulifera
- 8vgx – CpBPO – Cryo EM
- 7qvw – CpBPO (mutant)
- 7qwi – CpBPO + VO4
- 8vh0 – CpBPO + VO4 – Cryo EM
- 7qw3 – CpBPO (mutant) + Br
- 8vjq – CpBPO + VO4 + Br – Cryo EM
- 8vix – CpBPO + VO4 + O2 – Cryo EM
- 8q20, 8q21, 8q22 – AmBPO (mutant)
- Vanadium-containing iodoperoxidase
- 4cit, 4usz – IPO + VO4 – Zobellia galactanivorans
References
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