Evidence map›Paper›PMID 36721060›Full record

ArticleThe ISME journal2023

Unexpected complexity of the ammonia monooxygenase in archaea.

Logan H Hodgskiss, Michael Melcher, Melina Kerou, Weiqiang Chen, Rafael I Ponce-Toledo, Savvas N Savvides, Stefanie Wienkoop, Markus Hartl, Christa Schleper

Erratum issuedOpen access · hybridFull text read
In one paragraph

Article in The ISME journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

24 citing papers in PubMed, 48 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Logan H HodgskissArchaea Biology and Ecogenomics Unit, Department of Functional and Evolutionary Ecology, University of Vienna, Vienna, Austria.ORCID 0000-0002-8796-3840
Michael MelcherArchaea Biology and Ecogenomics Unit, Department of Functional and Evolutionary Ecology, University of Vienna, Vienna, Austria.
Melina KerouArchaea Biology and Ecogenomics Unit, Department of Functional and Evolutionary Ecology, University of Vienna, Vienna, Austria.ORCID 0000-0003-1657-3041
Weiqiang ChenMass Spectrometry Facility, Max Perutz Labs, Vienna BioCenter (VBC), Vienna, Austria.
Rafael I Ponce-ToledoArchaea Biology and Ecogenomics Unit, Department of Functional and Evolutionary Ecology, University of Vienna, Vienna, Austria.
Savvas N SavvidesVIB Center for Inflammation Center and Department of Biochemistry & Microbiology, Ghent University, Ghent, Belgium.ORCID 0000-0003-3420-5947
Stefanie WienkoopMolecular Systems Biology Unit, Department of Functional and Evolutionary Ecology, University of Vienna, Vienna, Austria.
Markus HartlMass Spectrometry Facility, Max Perutz Labs, Vienna BioCenter (VBC), Vienna, Austria.
Christa SchleperArchaea Biology and Ecogenomics Unit, Department of Functional and Evolutionary Ecology, University of Vienna, Vienna, Austria. christa.schleper@univie.ac.at.ORCID 0000-0002-1918-2735
University of Vienna · ATGhent University · BEMax Perutz Labs · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ammonia oxidation, as the first step of nitrification, constitutes a critical process in the global nitrogen cycle. However, fundamental knowledge of its key enzyme, the copper-dependent ammonia monooxygenase, is lacking, in particular for the environmentally abundant ammonia-oxidizing archaea (AOA). Here the structure of the enzyme is investigated by blue-native gel electrophoresis and proteomics from native membrane complexes of two AOA. Besides the known AmoABC subunits and the earlier predicted AmoX, two new protein subunits, AmoY and AmoZ, were identified. They are unique to AOA, highly conserved and co-regulated, and their genes are linked to other AMO subunit genes in streamlined AOA genomes. Modeling and in-gel cross-link approaches support an overall protomer structure similar to the distantly related bacterial particulate methane monooxygenase but also reveals clear differences in extracellular domains of the enzyme. These data open avenues for further structure-function studies of this ecologically important nitrification complex.

Indexed as

ArchaeaOxidoreductasesGene ExpressionNative Polyacrylamide Gel ElectrophoresisNitrificationPhylogenyammonia monooxygenaseOxidoreductases

Identifiers

PMID36721060
PMCPMC10030591
OpenAlexW4318700676

What OpenQuestion holds

Textfull text, public
LicenceCC BY
reference markers read6
measurements read33
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.