Evidence map›Paper›PMID 40127040›Full record

ArticleJournal of computational chemistry2025

The Mechanism of Nitrite Reductase.

Per E M Siegbahn

Abstract read
In one paragraph

Article in Journal of computational chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Nitrate-Nitrite Interplay in the Nitrogen Biocycle.Molecules (Basel, Switzerland) · 2025
    Review
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, Sweden.ORCID https://orcid.org/0000-0001-7787-1881

Funding

Swedish Research Council 2018-05973Swedish Research Council 2022-22-955
6 · The paper itself

Abstract

Cytochrome c nitrite reductase (CcNiR) activates nitrite and produces ammonia. It is one of several enzymes that use a redox-active cofactor to perform its reaction. In this case, the cofactor has a heme with a lysine as the proximal ligand and a charged nearby arginine. The role of a tyrosine, which is also close, has been less clear. There are also four bis-histidine-ligated hemes involved in the electron transfers. CcNiR has been studied before, using essentially the same methods as here. However, the mechanism is very complicated, involving six reductions, and quite different results for the mechanism have been obtained here. For example, the tyrosine has here been found to be redox active in the final step when ammonia is produced. Also, the arginine has here been found to stay protonated throughout the mechanism, which is different from what was found in the previous study. The present results are in very good agreement with experimental findings and are, therefore, another case where the methodology has been shown to work very well. Previous examples include Photosystem II and Nitrogenase, normally considered to be the most important enzymes in nature for the development of life.

Indexed as

Nitrate ReductasesNitrite ReductasesNitritesOxidation-ReductionNitrate ReductasesNitrite ReductasesNitritescytochrome c nitrite reductaseDFTmechanismsquantum chemistryredox enzymes

Identifiers

PMID40127040
PMCPMC11932435

What OpenQuestion holds

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Registered trials

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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.