Evidence map›Paper›PMID 39693510›Full record

ArticleThe journal of physical chemistry. B2025

Nitrification Mechanisms for the P460 Enzymes.

Per E M Siegbahn

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. The Intricate Mechanism of Nitric Oxide Synthase.Journal of computational chemistry · 2026
    Article
  2. Article
  3. The Mechanism of Nitrite Reductase.Journal of computational chemistry · 2025
    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

1 author.

Per E M SiegbahnDepartment of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm SE-106 91, Sweden.ORCID 0000-0001-7787-1881

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The oxidation of hydroxylamine was studied by quantum chemical modeling. Hydroxylamine is the product of ammonia oxidation in ammonia monooxygenase. That mechanism has been studied recently by quantum chemical modeling as here. Only two enzymes can oxidize hydroxylamine, hydroxylamine oxidase and cytochrome-P460. Both employ the unusual P460-heme cofactor. In hydroxylamine oxidase, there is a covalently linked tyrosine, while in cytochrome-P460, there is a covalently linked lysine. The calculations give explanations for the experimental findings that NO is the final product in hydroxylamine oxidase, while N

Indexed as

NitrificationOxidation-ReductionHydroxylamineModels, MolecularOxidoreductasesQuantum TheoryHydroxylamineOxidoreductases

Identifiers

PMID39693510
PMCPMC11726666

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.