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7M1J

Crystal structure of dehaloperoxidase B in complex with 2,6-dibromophenol

Summary for 7M1J
Entry DOI10.2210/pdb7m1j/pdb
DescriptorDehaloperoxidase B, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (6 entities in total)
Functional Keywordsheme peroxidase, peroxygenase, heme cofactor, oxygen binding, oxidoreductase
Biological sourceAmphitrite ornata
Total number of polymer chains2
Total formula weight32598.02
Authors
Ghiladi, R.A.,de Serrano, V.S.,Malewschik, T. (deposition date: 2021-03-13, release date: 2022-08-31, Last modification date: 2023-10-18)
Primary citationMalewschik, T.,Carey, L.M.,de Serrano, V.,Ghiladi, R.A.
Bridging the functional gap between reactivity and inhibition in dehaloperoxidase B from Amphitrite ornata: Mechanistic and structural studies with 2,4- and 2,6-dihalophenols.
J.Inorg.Biochem., 236:111944-111944, 2022
Cited by
PubMed Abstract: The multifunctional catalytic globin dehaloperoxidase (DHP) from the marine worm Amphitrite ornata was shown to catalyze the HO-dependent oxidation of 2,4- and 2,6-dihalophenols (DXP; X = F, Cl, Br). Product identification by LC-MS revealed multiple monomeric products with varying degrees of oxidation and/or dehalogenation, as well as oligomers with n up to 6. Mechanistic and O-labeling studies demonstrated sequential dihalophenol oxidation via peroxidase and peroxygenase activities. Binding studies established that 2,4-DXP (X = Cl, Br) have the highest affinities of any known DHP substrate. X-ray crystallography identified different binding positions for 2,4- and 2,6-DXP substrates in the hydrophobic distal pocket of DHP. Correlation between the number of halogens and the substrate binding orientation revealed a halogen-dependent binding motif for mono- (4-halophenol), di- (2,4- and 2,6-dihalophenol) and trihalophenols (2,4,6-trihalopenol). Taken together, the findings here on dihalophenol reactivity with DHP advance our understanding of how these compounds bridge the inhibitory and oxidative functions of their mono- and trihalophenol counterparts, respectively, and provide further insight into the protein structure-function paradigm relevant to multifunctional catalytic globins in comparison to their monofunctional analogs.
PubMed: 35969974
DOI: 10.1016/j.jinorgbio.2022.111944
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.554 Å)
Structure validation

239149

數據於2025-07-23公開中

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