Evidence map›Paper›PMID 37364353›Full record

ArticleJournal of inorganic biochemistry2023

Second-sphere tuning of analogues for the ferric-hydroperoxoheme form of Mycobacterium tuberculosis MhuD.

Kayla L Johnson, Amanda B Graves, Kaitlyn Eckhert, Matthew D Liptak

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 75% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 1 institution in 1 country.

Kayla L JohnsonDepartment of Chemistry, University of Vermont, 82 University Place, Burlington, VT 05405, United States of America.
Amanda B GravesDepartment of Chemistry, University of Vermont, 82 University Place, Burlington, VT 05405, United States of America.
Kaitlyn EckhertDepartment of Chemistry, University of Vermont, 82 University Place, Burlington, VT 05405, United States of America.
Matthew D LiptakDepartment of Chemistry, University of Vermont, 82 University Place, Burlington, VT 05405, United States of America. Electronic address: matthew.liptak@uvm.edu.
University of Vermont · US

Funding

Heme Oxygenases: chemically complex enzymes found in diverse biological pathwaysR35GM139516 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI Matthew D Liptak · 2021 to 2026
$1.7M
NIGMS NIH HHS R35 GM139516
6 · The paper itself

Abstract

Mycobacterium tuberculosis MhuD catalyzes the oxygenation of heme to mycobilin; experimental data presented here elucidates the novel hydroxylation reaction catalyzed by this enzyme. Analogues for the critical ferric-hydroperoxoheme (MhuD-heme-OOH) intermediate of this enzyme were characterized using UV/Vis absorption (Abs), circular dichroism (CD), and magnetic CD (MCD) spectroscopies. In order to extract electronic transition energies from these spectroscopic data, a novel global fitting model was developed for analysis of UV/Vis Abs, CD, and MCD data. A variant of MhuD was prepared, N7S, which weakens the affinity of heme-bound enzyme for a hydroperoxo analogue, azide, without significantly altering the protein secondary structure. Global fitting of spectroscopic data acquired in this study revealed that the second-sphere N7S substitution perturbs the electronic structure of two analogues for MhuD-heme-OOH: azide-inhibited MhuD (MhuD-heme-N

Indexed as

Mycobacterium tuberculosisAzidesHemeHeme Oxygenase (Decyclizing)IronLigandsAzidesHemeHeme Oxygenase (Decyclizing)IronLigandsCD spectroscopyGlobal fittingHeme oxygenaseMCD spectroscopyMhuDSecond-sphere interactions

Identifiers

PMID37364353
PMCPMC10332388
OpenAlexW4381194309

What OpenQuestion holds

Textmetadata
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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.