Evidence map›Paper›PMID 35259597›Full record

ArticleJournal of inorganic biochemistry2022

Mechanism of substrate inhibition in cytochrome-c dependent NO reductases from denitrifying bacteria (cNORs).

Hirotoshi Matsumura, Abayomi S Faponle, Peter-Leon Hagedoorn, Takehiko Tosha, Sam P de Visser, Pierre Moënne-Loccoz

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2022. 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
–field-weighted citation impact
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.

  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.

Hirotoshi MatsumuraDepartment of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, OR 97239, USA.
Abayomi S FaponleManchester Institute of Biotechnology, Department of Chemical Engineering and Analytical Science, The University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Peter-Leon HagedoornDepartment of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, the Netherlands.
Takehiko ToshaRIKEN SPring-8 Center, 1-1-1, Kouto, Sayo, Hyogo 679-5148, Japan.
Sam P de VisserManchester Institute of Biotechnology, Department of Chemical Engineering and Analytical Science, The University of Manchester, 131 Princess Street, Manchester M1 7DN, United Kingdom.
Pierre Moënne-LoccozDepartment of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health & Science University, 3181 SW Sam Jackson Park Road, Portland, OR 97239, USA. Electronic address: moennelo@ohsu.edu.

Funding

Nitric Oxide Reactions in MetalloenzymesR01GM074785 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MOENNE-LOCCOZ, PIERRE · 2006 to 2019
$3.8M
NIGMS NIH HHS R01 GM074785
6 · The paper itself

Abstract

Steady-state kinetics of cytochrome-c dependent denitrifying NO reductases (cNORs) show evidence of substrate inhibition at NO concentrations higher than 10 μM, but the mechanism of inhibition remains unclear. Here, we present low-temperature FTIR photolysis experiments carried out on the NO complex formed by addition of NO to the oxidized cNORs. A differential signal at 1261 cm

Indexed as

Ferric CompoundsHemeBacteriaCatalytic DomainCytochromesNADH DehydrogenaseCytochromesFerric CompoundsHemeNADH DehydrogenaseIron proteinsNitric oxide reductasesReaction mechanismsSpectroscopy

Identifiers

PMID35259597
PMCPMC9007887

What OpenQuestion holds

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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.