Evidence map›Paper›PMID 29170897›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2018

Selective tuning of activity in a multifunctional enzyme as revealed in the F21W mutant of dehaloperoxidase B from Amphitrite ornata.

Leiah M Carey, Kyung Beom Kim, Nikolette L McCombs, Paul Swartz, Cheal Kim, Reza A Ghiladi

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Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. Article
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

6 authors at 2 institutions in 2 countries.

Leiah M CareyDepartment of Chemistry, North Carolina State University, Raleigh, NC, 27695-8204, USA.
Kyung Beom KimDepartment of Chemistry, North Carolina State University, Raleigh, NC, 27695-8204, USA.
Nikolette L McCombsDepartment of Chemistry, North Carolina State University, Raleigh, NC, 27695-8204, USA.
Paul SwartzDepartment of Structural and Molecular Biochemistry, North Carolina State University, Raleigh, NC, 27695-7622, USA.
Cheal KimDepartment of Fine Chemistry, Seoul National University of Science and Technology, Seoul, 139-743, Korea.
Reza A GhiladiDepartment of Chemistry, North Carolina State University, Raleigh, NC, 27695-8204, USA. Reza_Ghiladi@ncsu.edu.ORCID 0000-0002-6450-9311
North Carolina State University · USSeoul National University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Possessing both peroxidase and peroxygenase activities with a broad substrate profile that includes phenols, indoles, and pyrroles, the enzyme dehaloperoxidase (DHP) from Amphitrite ornata is a multifunctional catalytic hemoglobin that challenges many of the assumptions behind the well-established structure-function paradigm in hemoproteins. While previous studies have demonstrated that the F21W variant leads to attenuated peroxidase activity in DHP, here we have studied the impact of this mutation on peroxygenase activity to determine if it is possible to selectively tune DHP to favor one function over another. Biochemical assays with DHP B (F21W) revealed minimal decreases in peroxygenase activity of 1.2-2.1-fold as measured by 4-nitrophenol or 5-Br-indole substrate conversion, whereas the peroxidase activity catalytic efficiency for 2,4,6-trichlorophenol (TCP) was more than sevenfold decreased. Binding studies showed a 20-fold weaker affinity for 5-bromoindole (K

Indexed as

MutationAnimalsCatalysisCrystallography, X-RayHemoglobinsPeroxidasesPolychaetaSpectrophotometry, UltravioletSubstrate SpecificityDHP I dehaloperoxidaseHemoglobinsPeroxidasesGlobinPeroxidasePeroxygenaseStructure–function relationship

Identifiers

PMID29170897
OpenAlexW2770716916

What OpenQuestion holds

Textmetadata
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.