Evidence map›Paper›PMID 33398888›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2021

HNO to NO Conversion Mechanism with Copper Zinc Superoxide Dismutase, Comparison with Heme Protein Mediated Conversions, and the Origin of Questionable Reversibility.

Yelu Shi, Matthew A Michael, Yong Zhang

Open access · greenAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

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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

3 authors at 1 institution in 2 countries.

Yelu ShiDepartment of Chemistry and Chemical Biology, Stevens Institute, of Technology, 1 Castle Point on Hudson, Hoboken, NJ, 07030, USA.
Matthew A MichaelDepartment of Chemistry and Chemical Biology, Stevens Institute, of Technology, 1 Castle Point on Hudson, Hoboken, NJ, 07030, USA.
Yong ZhangDepartment of Chemistry and Chemical Biology, Stevens Institute, of Technology, 1 Castle Point on Hudson, Hoboken, NJ, 07030, USA.ORCID http://orcid.org/0000-0001-7207-6416
Stevens Institute of Technology · US

Funding

Structure, Spectra, and Roles of Metal and Active Site in HNO Heme Protein CompleR15GM085774 · NIGMS · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI ZHANG, YONG · 2008 to 2021
$1.4M
National Institutes of Health GM085774NIGMS NIH HHS R15 GM085774NIH HHS GM085774
6 · The paper itself

Abstract

The interconversion of NO and HNO, via copper zinc superoxide dismutase (CuZnSOD), is important in biomedicine and for HNO detection. Many mechanistic questions, including the decades-long debate on reversibility, were resolved in this work. Calculations of various active-site and full-protein models show that the basic mechanism is proton-coupled electron transfer with a computed barrier of 10.98 kcal mol

Indexed as

HemeproteinsCopperNitrogen OxidesSuperoxide DismutaseZincCopperHemeproteinsNitrogen OxidesSuperoxide DismutaseZinccomputational chemistrycopperenzymesnitrogen oxidesreaction mechanisms

Identifiers

PMID33398888
PMCPMC7954974
OpenAlexW3119282808

What OpenQuestion holds

Textmetadata
LicenceTDM
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.