Nitrotoxin metabolism in bacteria may have emerged from a diverse oxidoreductase reservoir
- 1University of North Bengal
Abstract
Bacterial transformation of 3 nitropropionic acid (3NPA) is typically viewed through canonical nitronate monooxygenases (NMOs), yet sequence annotation poorly resolves function across this flavoprotein family. Here we show that the environmental YrpB/NMO associated oxidoreductase space is dominated by YrpB related proteins: across 13 metagenomes, 83.1% of 390 conserved domain supported candidates were YrpB-associated. Cultivation along an Eisenia fetida feed gut cast continuum recovered 31 phylogenetically diverse 3NPA responsive bacteria, revealing that this phenotype is distributed across multiple lineages. Using the previously genome-sequenced Serratia sp. EWG9 as a tractable exemplar, we demonstrate sustained 3NPA supported growth, 44% parent compound depletion and a broad early transcriptional reorganization. Its focal oxidoreductase OXR01 occupies overlapping YrpB/NMO sequence space and shows stable predicted 3NPA accommodation without strong transcriptional induction. These findings reposition canonical NMOs as one component of a broader, ecologically distributed oxidoreductase reservoir for bacterial nitrotoxin responsiveness.
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BibTeX
@misc{barman2026nitrotoxin,
title = {{Nitrotoxin metabolism in bacteria may have emerged from a diverse oxidoreductase reservoir}},
author = {P. Barman and S. Sinha and R. Chakraborty},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.13.751228},
url = {https://www.biorxiv.org/content/10.64898/2026.09.13.751228v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Nitrotoxin metabolism in bacteria may have emerged from a diverse oxidoreductase reservoir
AU - P. Barman
AU - S. Sinha
AU - R. Chakraborty
PY - 2026
DA - 2026/09/13
PB - bioRxiv
DO - 10.64898/2026.09.13.751228
UR - https://www.biorxiv.org/content/10.64898/2026.09.13.751228v1
AB - Bacterial transformation of 3 nitropropionic acid (3NPA) is typically viewed through canonical nitronate monooxygenases (NMOs), yet sequence annotation poorly resolves function across this flavoprotein family. Here we show that the environmental YrpB/NMO associated oxidoreductase space is dominated by YrpB related proteins: across 13 metagenomes, 83.1% of 390 conserved domain supported candidates were YrpB-associated. Cultivation along an Eisenia fetida feed gut cast continuum recovered 31 phylogenetically diverse 3NPA responsive bacteria, revealing that this phenotype is distributed across multiple lineages. Using the previously genome-sequenced Serratia sp. EWG9 as a tractable exemplar, we demonstrate sustained 3NPA supported growth, 44% parent compound depletion and a broad early transcriptional reorganization. Its focal oxidoreductase OXR01 occupies overlapping YrpB/NMO sequence space and shows stable predicted 3NPA accommodation without strong transcriptional induction. These findings reposition canonical NMOs as one component of a broader, ecologically distributed oxidoreductase reservoir for bacterial nitrotoxin responsiveness.
ER -