Unexpected complexity of the ammonia monooxygenase in archaea

Autor(en)

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

Abstrakt

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(en)

Department für Funktionelle und Evolutionäre Ökologie, Department für Biochemie und Zellbiologie

Externe Organisation(en)

Max F. Perutz Laboratories GmbH (MFPL), Ghent University , Medizinische Universität Wien

Journal

The ISME Journal

Band

17

Seiten

588-599

Anzahl der Seiten

12

ISSN

1751-7362

DOI

https://doi.org/10.1038/s41396-023-01367-3

Publikationsdatum

2023

Peer-reviewed

Ja

ÖFOS 2012

106022 Mikrobiologie

ASJC Scopus Sachgebiete

Ecology, Evolution, Behavior and Systematics, Microbiology

Link zum Portal

https://ucrisportal.univie.ac.at/de/publications/5a947962-7fe1-4725-987d-ea8b7f7426cb