Re-investigation of the HExxH enzyme DarF reveals a dehydrogenation–epoxidation reaction

2026/01/01 by Jabal Rahmat Haedar, Nils Böhringer, G. Swarna Kumari +6 · 1 voice
Chemistry · Energy · Biochemistry, Genetics and Molecular Biology · #Metal-Catalyzed Oxygenation Mechanisms #Metalloenzymes and iron-sulfur proteins #Porphyrin Metabolism and Disorders

paper · pdf · doi:10.1039/d6ob00496b

openalex publication_date 2026/01/01 · openalex created_date 2026/05/21 · openalex updated_date 2026/07/26

Abstract

Darobactin A is a potent antibiotic, but the biosynthesis of its derivative, dehydrodarobactin A, remains unclear. Here, we discovered HExxH enzyme DarF catalyzes a dehydrogenation-epoxidation reaction and linked to dehydrodarobactin A biosynthesis.

Citations

• Accurate structure prediction of biomolecular interactions with AlphaFold 3
• A Purely σ-Aromatic, Planar Ge 4 2+ -Ring

Discussions

• We re-investigated the HExxH enzyme DarF and proposed a dehydrogenation-epoxidation reaction. We linked DarF to the dehydrodarobactin A biosynthesis and proposed first epoxidized darobactin | Org Biom [bsky, 3 points, 0 comments]

Related

• From Binding to Catalysis: Emergence of a Rudimentary Enzyme Conferring Intrinsic Antibiotic Resistance
• Crystal structure of dihydroorotate dehydrogenase from Helicobacter pylori with bound flavin mononucleotide
• The family of berberine bridge enzyme-like enzymes: A treasure-trove of oxidative reactions
• Halogenases and dehalogenases: mechanisms, engineering, and applications
• Characterization and Mechanistic Study of a Radical SAM Dehydrogenase in the Biosynthesis of Butirosin