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The Selenoproteome as a Dynamic Response Mechanism to Oxidative Stress in Hydrogenotrophic Methanogenic Communities.
Kleikamp, Hugo B C; Palacios, Paola A; Kofoed, Michael V W; Papacharalampos, Georgios; Bentien, Anders; Nielsen, Jeppe L.
Affiliation
  • Kleikamp HBC; Department of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, 9220 Aalborg, Denmark.
  • Palacios PA; Department of Biological and Chemical Engineering, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus, Denmark.
  • Kofoed MVW; Department of Biological and Chemical Engineering, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus, Denmark.
  • Papacharalampos G; Department of Biological and Chemical Engineering, Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus, Denmark.
  • Bentien A; Department of Biological and Chemical Engineering, Aarhus University, Åbogade 40, 8200 Aarhus, Denmark.
  • Nielsen JL; Department of Chemistry and Bioscience, Aalborg University, Fredrik Bajers Vej 7H, 9220 Aalborg, Denmark.
Environ Sci Technol ; 58(15): 6637-6646, 2024 Apr 16.
Article in En | MEDLINE | ID: mdl-38580315
ABSTRACT
Methanogenesis is a critical process in the carbon cycle that is applied industrially in anaerobic digestion and biogas production. While naturally occurring in diverse environments, methanogenesis requires anaerobic and reduced conditions, although varying degrees of oxygen tolerance have been described. Microaeration is suggested as the next step to increase methane production and improve hydrolysis in digestion processes; therefore, a deeper understanding of the methanogenic response to oxygen stress is needed. To explore the drivers of oxygen tolerance in methanogenesis, two parallel enrichments were performed under the addition of H2/CO2 in an environment without reducing agents and in a redox-buffered environment by adding redox mediator 9,10-anthraquinone-2,7-disulfonate disodium. The cellular response to oxidative conditions is mapped using proteomic analysis. The resulting community showed remarkable tolerance to high-redox environments and was unperturbed in its methane production. Next to the expression of pathways to mitigate reactive oxygen species, the higher redox potential environment showed an increased presence of selenocysteine and selenium-associated pathways. By including sulfur-to-selenium mass shifts in a proteomic database search, we provide the first evidence of the dynamic and large-scale incorporation of selenocysteine as a response to oxidative stress in hydrogenotrophic methanogenesis and the presence of a dynamic selenoproteome.
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Full text: 1 Database: MEDLINE Main subject: Selenium / Euryarchaeota Language: En Journal: Environ Sci Technol Year: 2024 Type: Article Affiliation country: Denmark

Full text: 1 Database: MEDLINE Main subject: Selenium / Euryarchaeota Language: En Journal: Environ Sci Technol Year: 2024 Type: Article Affiliation country: Denmark