Investigation of central energy metabolism-related protein complexes of ANME-2d methanotrophic archaea by complexome profiling


Por: Berger S., Cabrera-Orefice A., Jetten M.S.M., Brandt U., Welte C.U.

Publicada: 1 ene 2021
Resumen:
The anaerobic oxidation of methane is important for mitigating emissions of this potent greenhouse gas to the atmosphere and is mediated by anaerobic methanotrophic archaea. In a ‘Candidatus Methanoperedens BLZ2’ enrichment culture used in this study, methane is oxidized to CO2 with nitrate being the terminal electron acceptor of an anaerobic respiratory chain. Energy conservation mechanisms of anaerobic methanotrophs have mostly been studied at metagenomic level and hardly any protein data is available at this point. To close this gap, we used complexome profiling to investigate the presence and subunit composition of protein complexes involved in energy conservation processes. All enzyme complexes and their subunit composition involved in reverse methanogenesis were identified. The membrane-bound enzymes of the respiratory chain, such as F420H2:quinone oxidoreductase, membrane-bound heterodisulfide reductase, nitrate reductases and Rieske cytochrome bc1 complex were all detected. Additional or putative subunits such as an octaheme subunit as part of the Rieske cytochrome bc1 complex were discovered that will be interesting targets for future studies. Furthermore, several soluble proteins were identified, which are potentially involved in oxidation of reduced ferredoxin produced during reverse methanogenesis leading to formation of small organic molecules. Taken together these findings provide an updated, refined picture of the energy metabolism of the environmentally important group of anaerobic methanotrophic archaea. © 2020 The Author(s)

Filiaciones:
Institute for Wetland and Water Research, Radboud University, Heyendaalseweg 135, Nijmegen, 6525 AJ, Netherlands
Molecular Bioenergetics Group, Radboud Institute for Molecular Life Sciences, Department of Pediatrics, Radboud University Medical Center, Geert-Grooteplein Zuid 10, Nijmegen, 6525 GA, Netherlands
ISSN: 00052728
Editorial
ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS, Países Bajos
Tipo de documento: Article
Volumen: 1862 Número: 1
Páginas:
WOS Id: 000601394200005
ID de PubMed: 33002447
imagen All Open Access, Hybrid Gold

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