Evidence map›Paper›PMID 24302732›Full record

ArticleThe Journal of biological chemistry2014

Structural basis of biological NO generation by octaheme oxidoreductases.

Wouter J Maalcke, Andreas Dietl, Sophie J Marritt, Julea N Butt, Mike S M Jetten, Jan T Keltjens, Thomas R M Barends, Boran Kartal

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.7field-weighted citation impact, top 7% of its field
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

45 citing papers in PubMed, 106 citations in OpenAlex.

  1. Article
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  4. Cytochromes P460 and c'-β: exploiting a novel fold for multiple functions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  15. Article
  16. NHMicrobes and environments · 2022
    Article
  17. Specificity of SmallACS omega · 2021
    Article
  18. Heme P460: A (Cross) Link to Nitric Oxide.Accounts of chemical research · 2020
    Article
  19. Multiheme hydroxylamine oxidoreductases produce NO during ammonia oxidation in methanotrophs.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. 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

8 authors at 4 institutions in 3 countries.

Wouter J MaalckeFrom the Department of Microbiology, Institute for Water and Wetland Research, Radboud University Nijmegen, 6525AJ Nijmegen, The Netherlands.
Andreas Dietl
Sophie J Marritt
Julea N Butt
Mike S M Jetten
Jan T Keltjens
Thomas R M Barends
Boran Kartal
Radboud University Nijmegen · NLMax Planck Institute for Medical Research · DENorwich Research Park · GBDelft University of Technology · NL

Funding

Biotechnology and Biological Sciences Research Council BB/G009228Biotechnology and Biological Sciences Research Council BB/G009228/1European Research Council 232937
6 · The paper itself

Abstract

Nitric oxide is an important molecule in all domains of life with significant biological functions in both pro- and eukaryotes. Anaerobic ammonium-oxidizing (anammox) bacteria that contribute substantially to the release of fixed nitrogen into the atmosphere use the oxidizing power of NO to activate inert ammonium into hydrazine (N2H4). Here, we describe an enzyme from the anammox bacterium Kuenenia stuttgartiensis that uses a novel pathway to make NO from hydroxylamine. This new enzyme is related to octaheme hydroxylamine oxidoreductase, a key protein in aerobic ammonium-oxidizing bacteria. By a multiphasic approach including the determination of the crystal structure of the K. stuttgartiensis enzyme at 1.8 Å resolution and refinement and reassessment of the hydroxylamine oxidoreductase structure from Nitrosomonas europaea, both in the presence and absence of their substrates, we propose a model for NO formation by the K. stuttgartiensis enzyme. Our results expand the understanding of the functions that the widespread family of octaheme proteins have.

Indexed as

AmmoniaBacterial ProteinsCrystallography, X-RayHydrazinesNitric OxideOxidation-ReductionOxidoreductasesPlanctomycetalesProtein Structure, TertiaryStructure-Activity RelationshipAmmoniaBacterial ProteinshydrazineHydrazinesNitric OxideOxidoreductasesAnaerobic Ammonium OxidationEnzyme KineticsEnzyme PurificationHydroxylamineNitric OxideNitrogen MetabolismOctaheme ProteinsProtein StructureReactive Nitrogen SpeciesX-ray Crystallography

Identifiers

PMID24302732
PMCPMC3894310
OpenAlexW2170390407

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.