Novel nitrite reductase domain structure suggests a chimeric denitrification repertoire in the phylum Chloroflexi
Name
MicrobiologyOpen - 2022 - Schwartz - Novel nitrite reductase domain structure suggests a chimeric denitrification.pdf
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Published version
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7.91 MB
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Adobe PDF
Checksum (MD5)
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Author(s)
Schwartz, Sarah L
Momper, Lily
Rangel, Luiz Thiberio
Magnabosco, Cara
Amend, Jan P
Fournier, Gregory P
Date Issued
2022
Journal
MicrobiologyOpen
Publisher
Wiley
Citation
Schwartz, Sarah L, Momper, Lily, Rangel, Luiz Thiberio, Magnabosco, Cara, Amend, Jan P et al. 2022. "Novel nitrite reductase domain structure suggests a chimeric denitrification repertoire in the phylum Chloroflexi." MicrobiologyOpen, 11 (1).
Version
Final published version
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.
MIT Department
Massachusetts Institute of Technology. Department of Earth, Atmospheric, and Planetary Sciences
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Creative Commons Attribution 4.0 International license
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DOI of Published Version
https://doi.org/10.1002/MBO3.1258
