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With the increased occurrences of wildfires worldwide, there has been an increase in scientific interest surrounding the chemistry of fire-derived "black" carbon (BC). Traditionally, wildfire research has assumed that condensed aromatic carbon (ConAC) is exclusively produced via combustion, and thus, ConAC is equated to BC. However, the lack of correlations between ConAC in soils or rivers and wildfire history suggests that ConAC may be produced non-pyrogenically. Here, we show quantitative evidence that this occurs during the oxidation of biomass with environmentally ubiquitous hydroxyl radicals. Pine wood boards exposed to iron nails and natural weather conditions for 12 years yielded a charcoal-like ConAC-rich material. ConAC was also produced during laboratory oxidations of pine, maple, and brown-rotted oak woods, as well as algae, corn root, and tree bark. Back-of-the-envelope calculations suggest that biomass oxidation could be producing massive non-pyrogenic ConAC fluxes to terrestrial and aquatic environments. These estimates (e.g., 163-182 Tg-ConAC/year to soils) are much higher than the estimated pyrogenic "BC" fluxes (e.g., 128 Tg-ConAC/year to soils) implying that environmental ConAC is primarily non-pyrogenic. This novel perspective suggests that wildfire research trajectories should shift to assessing non-pyrogenic ConAC sources and fluxes, developing new methods for quantifying true BC, and establishing a new view of ConAC as an intermediate species in the biogeochemical processing of biomass during soil humification, aquatic photochemistry, microbial degradation, or mineral-organic matter interactions. We also advise against using BC or pyrogenic carbon (pyC) terminologies for ConAC measured in environmental matrices, unless a pyrogenic source can be confidently assigned.

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a large and diverse class of natural products of ribosomal origin. In the past decade, various sophisticated machine-learning-based software packages have been established to discover novel RiPPs that do not resemble the known families. Here, we show that tailoring enzymes that cluster with various RiPP families can serve as effective bioinformatic seeds, providing a complementary approach for novel RiPP discovery. Leveraging the fact that O -methyltransferases homologous to protein isoaspartyl methyltransferases (PIMTs) are associated with lasso peptide, graspetide, and lanthipeptide biosynthetic gene clusters (BGCs), we utilized a C-terminal motif unique to RiPP-associated O -methyltransferases as the search query to discover a novel family of RiPPs, the imiditides. Our genome-mining algorithm reveals a total of 670 imiditide BGCs, distributed across Gram-positive bacterial genomes. In addition, we demonstrate the heterologous production of the founding member of the imiditide family, mNmaA M , encoded in the genome of Nonomuraea maritima . In contrast to other RiPP-associated PIMTs that recognize constrained peptides as substrates, the PIMT homologue in the mNmaA M BGC, NmaM, methylates a specific Asp residue on the linear precursor peptide, NmaA. The methyl ester is then turned into an aspartimide spontaneously. Substrate specificity is achieved by extensive charge-charge interactions between the precursor NmaA and the modifying enzyme NmaM suggested by both experiments and an AlphaFold model prediction. Our study shows that PIMT-mediated aspartimide formation is an emerging backbone modification strategy in the biosynthesis of multiple RiPP families.