Evidence map›Paper›PMID 20545299›Full record

ArticleBiochemistry2010

Spectroscopic and mechanistic investigations of dehaloperoxidase B from Amphitrite ornata.

Jennifer D'Antonio, Edward L D'Antonio, Matthew K Thompson, Edmond F Bowden, Stefan Franzen, Tatyana Smirnova, Reza A Ghiladi

Abstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.9field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
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  4. Review
  5. 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 · 2018
    Article
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  12. Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011
    Article
  13. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Jennifer D'AntonioDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina 27695-8204, USA.
Edward L D'Antonio
Matthew K Thompson
Edmond F Bowden
Stefan Franzen
Tatyana Smirnova
Reza A Ghiladi
North Carolina State University · US

Funding

Molecular Biotechnology Training at North Carolina State UniversityT32GM008776 · NIGMS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI KELLY, ROBERT M · 2000 to 2019
$3.9M
NIGMS NIH HHS T32 GM008776
6 · The paper itself

Abstract

Dehaloperoxidase (DHP) from the terebellid polychaete Amphitrite ornata is a bifunctional enzyme that possesses both hemoglobin and peroxidase activities. Of the two DHP isoenzymes identified to date, much of the recent focus has been on DHP A, whereas very little is known pertaining to the activity, substrate specificity, mechanism of function, or spectroscopic properties of DHP B. Herein, we report the recombinant expression and purification of DHP B, as well as the details of our investigations into its catalytic cycle using biochemical assays, stopped-flow UV-visible, resonance Raman, and rapid freeze-quench electron paramagnetic resonance spectroscopies, and spectroelectrochemistry. Our experimental design reveals mechanistic insights and kinetic descriptions of the dehaloperoxidase mechanism which have not been previously reported for isoenzyme A. Namely, we demonstrate a novel reaction pathway in which the products of the oxidative dehalogenation of trihalophenols (dihaloquinones) are themselves capable of inducing formation of oxyferrous DHP B, and an updated catalytic cycle for DHP is proposed. We further demonstrate that, unlike the traditional monofunctional peroxidases, the oxyferrous state in DHP is a peroxidase-competent starting species, which suggests that the ferric oxidation state may not be an obligatory starting point for the enzyme. The data presented herein provide a link between the peroxidase and oxygen transport activities which furthers our understanding of how this bifunctional enzyme is able to unite its two inherent functions in one system.

Indexed as

AnimalsCloning, MolecularHalogenationHemoglobinsIronKineticsOxidation-ReductionOxygenPeroxidasesPolychaetaSpectrum AnalysisHemoglobinsIronOxygenPeroxidases

Identifiers

PMID20545299
PMCPMC2921985
OpenAlexW1993618540

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.