ArticleBiophysical journal2010
Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 59 citations in OpenAlex.
- Less is more: miniaturized heme enzymes with broad reactivity.Chemical science · 2026Review
- The Multifunctional Catalytic Hemoglobin fromMethods and protocols · 2024Article
- Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase.International journal of molecular sciences · 2023Article
- Carbon-fluorine bond cleavage mediated by metalloenzymes.Chemical Society reviews · 2020Review
- Unraveling the structural and chemical features of biological short hydrogen bonds.Chemical science · 2019Article
- Selective tuning of activity in a multifunctional enzyme as revealed in the F21W mutant of dehaloperoxidase B from Amphitrite ornata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Oxidation of Pyrrole by Dehaloperoxidase-Hemoglobin: Chemoenzymatic Synthesis of Pyrrolin-2-Ones.Catalysis science & technology · 2017Article
- Peroxygenase and oxidase activities of dehaloperoxidase-hemoglobin from Amphitrite ornata.Journal of the American Chemical Society · 2014Article
- A model for the flexibility of the distal histidine in dehaloperoxidase-hemoglobin A based on X-ray crystal structures of the carbon monoxide adduct.Biochemistry · 2014Article
- Complex of myoglobin with phenol bound in a proximal cavity.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Spectroscopic and mechanistic investigations of dehaloperoxidase B from Amphitrite ornata.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dehaloperoxidase (DHP) from the annelid Amphitrite ornata is a catalytically active hemoglobin-peroxidase that possesses a unique internal binding cavity in the distal pocket above the heme. The previously published crystal structure of DHP shows 4-iodophenol bound internally. This led to the proposal that the internal binding site is the active site for phenol oxidation. However, the native substrate for DHP is 2,4,6-tribromophenol, and all attempts to bind 2,4,6-tribromophenol in the internal site under physiological conditions have failed. Herein, we show that the binding of 4-halophenols in the internal pocket inhibits enzymatic function. Furthermore, we demonstrate that DHP has a unique two-site competitive binding mechanism in which the internal and external binding sites communicate through two conformations of the distal histidine of the enzyme, resulting in nonclassical competitive inhibition. The same distal histidine conformations involved in DHP function regulate oxygen binding and release during transport and storage by hemoglobins and myoglobins. This work provides further support for the hypothesis that DHP possesses an external binding site for substrate oxidation, as is typical for the peroxidase family of enzymes.
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