Unexpected complexity of the ammonia monooxygenase in archaea
- Author(s)
- Logan H Hodgskiss, Michael Melcher, Melina Kerou, Weiqiang Chen, Rafael I Ponce-Toledo, Savvas N Savvides, Stefanie Wienkoop, Markus Hartl, Christa Schleper
- 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.
- Organisation(s)
- Functional and Evolutionary Ecology, Department of Biochemistry and Cell Biology
- External organisation(s)
- Max F. Perutz Laboratories GmbH (MFPL), Ghent University , Medizinische Universität Wien
- Journal
- The ISME Journal
- Volume
- 17
- Pages
- 588-599
- No. of pages
- 12
- ISSN
- 1751-7362
- DOI
- https://doi.org/10.1038/s41396-023-01367-3
- Publication date
- 2023
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 106022 Microbiology
- ASJC Scopus subject areas
- Ecology, Evolution, Behavior and Systematics, Microbiology
- Portal url
- https://ucris.univie.ac.at/portal/en/publications/unexpected-complexity-of-the-ammonia-monooxygenase-in-archaea(5a947962-7fe1-4725-987d-ea8b7f7426cb).html