Unexpected complexity of the ammonia monooxygenase in archaea.
Journal
The ISME journal
ISSN: 1751-7370
Titre abrégé: ISME J
Pays: England
ID NLM: 101301086
Informations de publication
Date de publication:
04 2023
04 2023
Historique:
received:
08
07
2022
accepted:
12
01
2023
revised:
09
01
2023
pubmed:
1
2
2023
medline:
24
3
2023
entrez:
31
1
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 36721060
doi: 10.1038/s41396-023-01367-3
pii: 10.1038/s41396-023-01367-3
pmc: PMC10030591
doi:
Substances chimiques
ammonia monooxygenase
EC 1.7.3.-
Ammonia
7664-41-7
Oxidoreductases
EC 1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
588-599Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2023. The Author(s).
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