ArticleThe Journal of biological chemistry2026
Crystal structure of RohS, a heme-oxygenase-like N-oxygenase from azomycin biosynthesis.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Acinetobacter baumannii utilizes a novel protective factor to combat desiccation-induced oxidative stress.PloS one · 2026Article
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4 authors.
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Abstract
The nitro group is an important functional group found in the nitroimidazoles, antibiotic therapeutics for anaerobic pathogens. In the biosynthetic pathway to the nitroimidazole antibiotic azomycin, a nitro-forming enzyme RohS-a member of the heme-oxygenase-like dimetal/domain-containing oxidase/oxygenase (HDO) family-catalyzes a six-electron oxidation of 2-aminoimidazole to 2-nitroimidazole. Here, we present the 2.20 Å resolution crystal structure of RohS and identify a potential active site pocket consisting of seven key residues important for metal coordination. By comparing the structures and sequences of two RohS homologs-one functionally active and one inactive-we convert the inactive RohS to its active form, thus revealing a key residue for metal coordination in RohS catalysis. Altogether, our work provides a structural basis for further mechanistic investigation of this six-electron oxidation process and provides insight into the expanding repertoire of the HDO protein family and nitro-formation N-oxygenases.
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