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Novel nitrite reductase domain structure suggests a chimeric denitrification repertoire in the phylum Chloroflexi.
Schwartz, Sarah L; Momper, Lily; Rangel, Luiz Thiberio; Magnabosco, Cara; Amend, Jan P; Fournier, Gregory P.
Affiliation
  • Schwartz SL; Microbiology Graduate Program, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
  • Momper L; Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
  • Rangel LT; Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
  • Magnabosco C; Exponent Inc., Pasadena, California, USA.
  • Amend JP; Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
  • Fournier GP; Department of Earth Sciences, ETH Zurich, Zurich, Switzerland.
Microbiologyopen ; 11(1): e1258, 2022 02.
Article in En | MEDLINE | ID: mdl-35212484
ABSTRACT
Denitrification plays a central role in the global nitrogen cycle, reducing and removing nitrogen from marine and terrestrial ecosystems. The flux of nitrogen species through this pathway has a widespread impact, affecting ecological carrying capacity, agriculture, and climate. Nitrite reductase (Nir) and nitric oxide reductase (NOR) are the two central enzymes in this pathway. Here we present a previously unreported Nir domain architecture in members of phylum Chloroflexi. Phylogenetic analyses of protein domains within Nir indicate that an ancestral horizontal transfer and fusion event produced this chimeric domain architecture. We also identify an expanded genomic diversity of a rarely reported NOR subtype, eNOR. Together, these results suggest a greater diversity of denitrification enzyme arrangements exist than have been previously reported.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxidoreductases / Chloroflexi / Nitrite Reductases Language: En Journal: Microbiologyopen Year: 2022 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Oxidoreductases / Chloroflexi / Nitrite Reductases Language: En Journal: Microbiologyopen Year: 2022 Document type: Article Affiliation country: United States