Internal Binding of Halogenated Phenols in Dehaloperoxidase-Hemoglobin Inhibits Peroxidase Function (Q27664264)

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Michael F Davis

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Vesna de Serrano

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Francesco P Nicoletti

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Barry D Howes

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Stefan Franzen

Structure of dehaloperoxidase B at 1.58 Å resolution and structural characterization of the AB dimer fromAmphitrite ornata

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language of work or name

English

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publication date

8 September 2010

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published in

Biophysical Journal

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volume

99

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issue

5

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page(s)

1586-95

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cites work

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X-ray crystal structural analysis of the binding site in the ferric and oxyferrous forms of the recombinant heme dehaloperoxidase cloned from Amphitrite ornata

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New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornata

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Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes

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Determination of separate inhibitor and substrate binding sites in the dehaloperoxidase-hemoglobin from Amphitrite ornata

2 June 2018

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Different modes of binding of mono-, di-, and trihalogenated phenols to the hemoglobin dehaloperoxidase from Amphitrite ornata

27 November 2018

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Substrate binding triggers a switch in the iron coordination in dehaloperoxidase from Amphitrite ornata: HYSCORE experiments

27 November 2018

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27 November 2018

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Proximal cavity, distal histidine, and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase

27 November 2018

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Enzyme function of the globin dehaloperoxidase from Amphitrite ornata is activated by substrate binding

27 November 2018

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An enzymatic globin from a marine worm

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