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Investigate the catalytic function and activation pathway of recombinant globin dehaloperoxidase from Amphitrite ornata during the oxidation of halogenated phenols.

November 9, 2005Biochemistry

Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding

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Investigate the catalytic function and activation pathway of recombinant globin dehaloperoxidase from Amphitrite ornata during the oxidation of halogenated phenols.
Cloned, expressed, and purified recombinant Amphitrite ornata dehaloperoxidase (DHP).
Performed stopped-flow kinetic assays to measure the oxidative debromination of 2,4,6-tribromophenol (TBP) by ferric DHP in the presence of peroxide.
Ferric recombinant DHP exhibited catalytic activity intermediate between that of horseradish peroxidase and horse heart myoglobin.
Catalytic turnover required 2,4,6-tribromophenol to bind to the enzyme prior to the introduction of the peroxide cosubstrate, confirming an obligatory ordered two-electron oxidation mechanism.

Authors

JBJennifer BelyeaUniversity of North Carolina at Chapel Hill LGLauren B. G. GilveyNorth Carolina State University MDM.F. DavisLe Moyne College

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Implication

Biochemical analysis reveals substrate-mediated activation of recombinant dehaloperoxidase in Amphitrite ornata, indicating an obligatory binding order for two-electron oxidation.

Cite This Study

Belyea et al. (2005) studied this question.

synapsesocial.com/papers/6a7dff93fd5c83ea4ea1489d https://doi.org/10.1021/bi051731k

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Implication

Biochemical analysis reveals substrate-mediated activation of recombinant dehaloperoxidase in Amphitrite ornata, indicating an obligatory binding order for two-electron oxidation.

Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding

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Discussion

Implication

Cite This Study

Enzyme Function of the Globin Dehaloperoxidase from Amphitrite ornata Is Activated by Substrate Binding

Key Points

Discussion

Implication

Cite This Study

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