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Novel nitrite reductase domain structure suggests a chimeric denitrification repertoire in Phylum Chloroflexi
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  • Sarah Schwartz,
  • Lily Momper,
  • L. Thiberio Rangel,
  • Cara Magnabosco,
  • Jan Amend,
  • Gregory Fournier
Sarah Schwartz
Massachusetts Institute of Technology
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Lily Momper
Massachusetts Institute of Technology
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L. Thiberio Rangel
Massachusetts Institute of Technology
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Cara Magnabosco
ETH Zurich
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Jan Amend
University of Southern California
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Gregory Fournier
Massachusetts Institute of Technology
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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 nitric oxide reductase subtype, eNOR. Together, these results suggest a greater diversity of denitrification enzyme arrangements exist than have been previously reported.

Peer review status:IN REVISION

30 Apr 2021Submitted to MicrobiologyOpen
30 Apr 2021Assigned to Editor
30 Apr 2021Submission Checks Completed
07 May 2021Reviewer(s) Assigned
07 Jun 2021Review(s) Completed, Editorial Evaluation Pending
11 Jun 2021Editorial Decision: Revise Minor