Evidence map›Paper›PMID 37406385›Full record

ArticleJournal of inorganic biochemistry2023

Crystal structural investigations of heme protein derivatives resulting from reactions of aryl- and alkylhydroxylamines with human hemoglobin.

Samantha M Powell, Bing Wang, Viridiana E Herrera, Kiana Y Prather, Nancy T Nguyen, Erwin G Abucayon, Leonard M Thomas, Martin K Safo, George B Richter-Addo

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
0.2field-weighted citation impact, top 43% 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, 1 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

9 authors at 4 institutions in 1 country.

Samantha M PowellPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA; Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Bing WangPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA.
Viridiana E HerreraPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA; Department of Chemistry and Physics, Ivory V. Nelson Science Center, Lincoln University, Lincoln University, PA, 19352, USA.
Kiana Y PratherPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA; University of Oklahoma College of Medicine, 800 Stanton L. Young Blvd, Oklahoma City, OK 73117, USA.
Nancy T NguyenPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA; University of Oklahoma College of Medicine, 800 Stanton L. Young Blvd, Oklahoma City, OK 73117, USA.
Erwin G AbucayonPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA.
Leonard M ThomasPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA.
Martin K SafoDepartment of Medicinal Chemistry, School of Pharmacy and Institute for Structural Biology, Drug Discovery and Development, Virginia Commonwealth University, 800 East Leigh Street, Richmond, VA 23219, USA.
George B Richter-AddoPrice Family Foundation Institute of Structural Biology, Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019, USA. Electronic address: grichteraddo@ou.edu.
University of Oklahoma · USLincoln University - Pennsylvania · USPacific Northwest National Laboratory · USVirginia Commonwealth University · US

Funding

Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI THOMAS, LEONARD M · 2012 to 2021
$20.4M
NIGMS NIH HHS P20 GM103640
6 · The paper itself

Abstract

Phenylhydroxylamine (PhNHOH) and nitrosobenzene (PhNO) interact with human tetrameric hemoglobin (Hb) to form the nitrosobenzene adduct Hb(PhNO). These interactions also frequently lead to methemoglobin formation in red blood cells. We utilize UV-vis spectroscopy and X-ray crystallography to identify the primary and secondary products that form when PhNHOH and related alkylhydroxylamines (RNHOH; R = Me, t-Bu) react with human ferric Hb. We show that with MeNHOH, the primary product is Hb[α-Fe

Indexed as

Ferric CompoundsHemeproteinsFerrous CompoundsHemeHemoglobinsHumansNitroso CompoundsSolventsFerric CompoundsFerrous CompoundsHemeHemeproteinsHemoglobinsnitrosobenzeneNitroso CompoundsSolventsCrystallographyHemeHemichromeHemoglobinNitrosoalkaneNitrosobenzene

Identifiers

PMID37406385
PMCPMC10348690
OpenAlexW4381952013

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.