Evidence map›Paper›PMID 34267357›Full record

ArticleNature microbiology2021

Structural and functional characterization of the intracellular filament-forming nitrite oxidoreductase multiprotein complex.

Tadeo Moreno Chicano, Lea Dietrich, Naomi M de Almeida, Mohd Akram, Elisabeth Hartmann, Franziska Leidreiter, Daniel Leopoldus, Melanie Mueller, Ricardo Sánchez, Guylaine H L Nuijten and 9 more

Open access · hybridAbstract read
In one paragraph

Article in Nature microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 77 citations in OpenAlex.

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  6. Nitrate-Nitrite Interplay in the Nitrogen Biocycle.Molecules (Basel, Switzerland) · 2025
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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

19 authors at 6 institutions in 2 countries.

Tadeo Moreno Chicano *Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
Lea Dietrich *Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Naomi M de Almeida *Department of Microbiology, Radboud University, Nijmegen, the Netherlands.
Mohd AkramDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
Elisabeth HartmannDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
Franziska LeidreiterDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-8261-7359
Daniel LeopoldusDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-2974-0304
Melanie MuellerDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
Ricardo SánchezDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Guylaine H L NuijtenDepartment of Microbiology, Radboud University, Nijmegen, the Netherlands.
Joachim ReimannDepartment of Microbiology, Radboud University, Nijmegen, the Netherlands.
Kerstin-Anikó SeifertDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.
Ilme SchlichtingDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-0936-7496
Laura van NiftrikDepartment of Microbiology, Radboud University, Nijmegen, the Netherlands.ORCID http://orcid.org/0000-0002-7011-7234
Mike S M JettenDepartment of Microbiology, Radboud University, Nijmegen, the Netherlands.
Andreas DietlDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany. Andreas.Dietl@mpimf-heidelberg.mpg.de.
Boran KartalMicrobial Physiology Group, Max Planck Institute for Marine Microbiology, Bremen, Germany. bkartal@mpi-bremen.de.
Kristian PareyDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany. Kristian.Parey@biophys.mpg.de.
Thomas R M BarendsDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany. Thomas.Barends@mpimf-heidelberg.mpg.de.ORCID http://orcid.org/0000-0002-9488-3005
Max Planck Institute for Medical Research · DERadboud University Nijmegen · NLConstructor University · DEGoethe University Frankfurt · DEMax Planck Institute of Biophysics · DEOsnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitrate is an abundant nutrient and electron acceptor throughout Earth's biosphere. Virtually all nitrate in nature is produced by the oxidation of nitrite by the nitrite oxidoreductase (NXR) multiprotein complex. NXR is a crucial enzyme in the global biological nitrogen cycle, and is found in nitrite-oxidizing bacteria (including comammox organisms), which generate the bulk of the nitrate in the environment, and in anaerobic ammonium-oxidizing (anammox) bacteria which produce half of the dinitrogen gas in our atmosphere. However, despite its central role in biology and decades of intense study, no structural information on NXR is available. Here, we present a structural and biochemical analysis of the NXR from the anammox bacterium Kuenenia stuttgartiensis, integrating X-ray crystallography, cryo-electron tomography, helical reconstruction cryo-electron microscopy, interaction and reconstitution studies and enzyme kinetics. We find that NXR catalyses both nitrite oxidation and nitrate reduction, and show that in the cell, NXR is arranged in tubules several hundred nanometres long. We reveal the tubule architecture and show that tubule formation is induced by a previously unidentified, haem-containing subunit, NXR-T. The results also reveal unexpected features in the active site of the enzyme, an unusual cofactor coordination in the protein's electron transport chain, and elucidate the electron transfer pathways within the complex.

Indexed as

BacteriaBacterial ProteinsCatalytic DomainCryoelectron MicroscopyCrystallography, X-RayKineticsMultiprotein ComplexesNitratesNitritesOxidation-ReductionOxidoreductasesBacterial ProteinsMultiprotein ComplexesNitratesNitritesOxidoreductases

Identifiers

PMID34267357
PMCPMC8387239
OpenAlexW3180063203

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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.