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TitleComplexes of dual-function hemoglobin/dehaloperoxidase with substrate 2,4,6-trichlorophenol are inhibitory and indicate binding of halophenol to compound I.
Journal, issue, pagesBiochemistry, Vol. 52, Page 6203-6210, Year 2013
Publish dateMay 8, 2013 (structure data deposition date)
AuthorsWang, C. / Lovelace, L.L. / Sun, S. / Dawson, J.H. / Lebioda, L.
External linksBiochemistry / PubMed:23952341
MethodsX-ray diffraction
Resolution1.44 - 1.79 Å
Structure data

PDB-4kmv:
Structure of the L100F MUTANT OF DEHALOPEROXIDASE-HEMOGLOBIN A FROM AMPHITRITE ORNATA WITH 2,4,6-TRICHLOROPHENOL
Method: X-RAY DIFFRACTION / Resolution: 1.44 Å

PDB-4kmw:
Structure of the Y34N MUTANT OF DEHALOPEROXIDASE-HEMOGLOBIN A FROM AMPHITRITE ORNATA WITH 2,4,6-TRICHLOROPHENOL
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-4kn3:
Structure of the Y34NS91G double mutant of Dehaloperoxidase from Amphitrite ornata with 2,4,6-trichlorophenol
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-T6C:
2,4,6-trichlorophenol

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • amphitrite ornata (invertebrata)
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / GLOBIN / OXYGEN STORAGE / PEROXIDASE / OXIDOREDUCTASE / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex

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