ArticleFEBS open bio2012
Nitric oxide, substrate of Euphorbia characias peroxidase, switches off the CN(-) inhibitory effect.
Article in FEBS open bio, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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.
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.
Who cites it
2 citing papers in PubMed, 6 citations in OpenAlex.
- Effectiveness of isosorbide dinitrate in cyanide poisoning as a function of the administration timing.BMC pharmacology & toxicology · 2017Article
- Euphorbia characias latex amine oxidase and peroxidase: interacting enzymes?The protein journal · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oxidation of nitric oxide (NO) by Euphorbia characias latex peroxidase (ELP-Fe(III)), in the presence or in the absence of added calcium, has been investigated. The addition of hydrogen peroxide to the native enzyme leads to the formation of Compound I and serves to catalyse the NO oxidation. The addition of NO to Compound I leads to the formation of Compound II and, afterwards, to the native enzyme spectrum. Under anaerobic conditions, the incubation of the native enzyme (ELP-Fe(III))with NO leads to the formation of the stable complex, showing a characteristic absorption spectrum (ELP-Fe(II)-NO(+)). The rate of the formation of this complex is slower in the presence of calcium than in its absence, and the same applies to the rate of the formation of Compound II from Compound I, using NO as substrate. Finally, we demonstrate that NO protects ELP from the inactivation caused by CN(-) via a mechanism presumably requiring the formation of an enzyme-nitrosyl cyanide complex.
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Registered trials
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