Evidence map›Paper›PMID 38850249›Full record

ArticleThe journal of physical chemistry. B2024

Mechanisms for Methane and Ammonia Oxidation by Particulate Methane Monooxygenase.

Per E M Siegbahn

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2024. 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
–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

5 citing papers in PubMed.

  1. The Intricate Mechanism of Nitric Oxide Synthase.Journal of computational chemistry · 2026
    Article
  2. Oxygen Isotopic Fractionation of OACS environmental Au · 2026
    Article
  3. Article
  4. The Mechanism of Nitrite Reductase.Journal of computational chemistry · 2025
    Article
  5. Nitrification Mechanisms for the P460 Enzymes.The journal of physical chemistry. B · 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, SE-106 91 Stockholm, Sweden.ORCID 0000-0001-7787-1881

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Particulate MMO (pMMO) catalyzes the oxidation of methane to methanol and also ammonia to hydroxylamine. Experimental characterization of the active site has been very difficult partly because the enzyme is membrane-bound. However, recently, there has been major progress mainly through the use of cryogenic electron microscopy (cryoEM). Electron paramagnetic resonance (EPR) and X-ray spectroscopy have also been employed. Surprisingly, the active site has only one copper. There are two histidine ligands and one asparagine ligand, and the active site is surrounded by phenyl alanines but no charged amino acids in the close surrounding. The present study is the first quantum chemical study using a model of that active site (Cu

Indexed as

AmmoniaMethaneOxidation-ReductionOxygenasesCatalytic DomainElectron Spin Resonance SpectroscopyModels, MolecularAmmoniaMethanemethane monooxygenaseOxygenases

Identifiers

PMID38850249
PMCPMC11194816

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.