@article {Wei2025-rn,
	title = {Structure and mechanism of the azomycin biosynthetic enzyme {RohQ} that catalyzes a spontaneous cyclodehydration},
	journal = {J. Am. Chem. Soc.},
	volume = {147},
	number = {29},
	year = {2025},
	pages = {25117{\textendash}25122},
	publisher = {American Chemical Society (ACS)},
	abstract = {RohQ from the azomycin biosynthetic pathway catalyzes a spontaneous cyclodehydration to form 2-aminoimidazole. Here we report the structure and mechanism of RohQ and use a serendipitously bound imidazole to pinpoint active site residues. We propose that catalysis occurs at the dimeric interface using two key aspartic acid residues for proton transfer steps to accelerate 3 $\times$ 104-fold intramolecular cyclization of a guanidino group and aldehyde, releasing water. Our work expands our understanding of de novo emerged enzymes and provides the first structural and mechanistic view of a yet-unexplored protein family.},
	author = {Wei, Zi-Wang and Daniel-Ivad, Phillip and Zhang, Li and Ryan, Katherine S}
}
