Dehaloperoxidase

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<StructureSection load='4fh6' size='350' side='right' caption='Dehaloperoxidase heme-containing dimer complex with iodophenol and sulfate ions (PDB entry [[1ewa]])' scene=''>
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<StructureSection load='4fh6' size='350' side='right' caption='Dehaloperoxidase heme-containing dimer complex with tribromophenol, O2 and sulfate ions (PDB entry [[4fh6]])' scene=''>
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'''Dehaloperoxidase''' (DHP) is a heme-containing globin possessing peroxidase enzymatic activity. DHP catalyzes the peroxide-dependent dehalogenation of halophenol. DHP A and DHP B are isoenzymes of DHP.<ref>PMID:24791647</ref>
'''Dehaloperoxidase''' (DHP) is a heme-containing globin possessing peroxidase enzymatic activity. DHP catalyzes the peroxide-dependent dehalogenation of halophenol. DHP A and DHP B are isoenzymes of DHP.<ref>PMID:24791647</ref>
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== Structural highlights ==
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Tribromophenol and an O2 molecule are seen in the heme-containing active site.
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==3D structures of dehaloperoxidase==
==3D structures of dehaloperoxidase==

Revision as of 12:11, 22 December 2015

Dehaloperoxidase heme-containing dimer complex with tribromophenol, O2 and sulfate ions (PDB entry 4fh6)

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3D structures of dehaloperoxidase

Updated on 22-December-2015

References

  1. Barrios DA, D'Antonio J, McCombs NL, Zhao J, Franzen S, Schmidt AC, Sombers LA, Ghiladi RA. Peroxygenase and oxidase activities of dehaloperoxidase-hemoglobin from Amphitrite ornata. J Am Chem Soc. 2014 Jun 4;136(22):7914-25. doi: 10.1021/ja500293c. Epub 2014 May , 21. PMID:24791647 doi:http://dx.doi.org/10.1021/ja500293c

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