ArticleBiochemistry2024
Initial Steps in Methanobactin Biosynthesis: Substrate Binding by the Mixed-Valent Diiron Enzyme MbnBC.
Article in Biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026Article
- The Heme Oxygenase-Like Diiron Enzyme HrmI Reveals Altered Regulatory Mechanisms for Dioxygen Activation and Substrate N-Oxygenation.Journal of the American Chemical Society · 2025Article
- Copper-chelating natural products.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- OJournal of the American Chemical Society · 2025Article
- A multi-iron enzyme installs copper-binding oxazolone/thioamide pairs on a nontypeableProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications.Current opinion in chemical biology · 2024Review
- Purification and biochemical characterization of methanobactin biosynthetic enzymes.Methods in enzymology · 2024Article
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Authors and funding
7 authors.
Funding
Abstract
The MbnBC enzyme complex converts cysteine residues in a peptide substrate, MbnA, to oxazolone/thioamide groups during the biosynthesis of copper chelator methanobactin (Mbn). MbnBC belongs to the mixed-valent diiron oxygenase (MVDO) family, of which members use an Fe(II)Fe(III) cofactor to react with dioxygen for substrate modification. Several crystal structures of the inactive Fe(III)Fe(III) form of MbnBC alone and in complex with MbnA have been reported, but a mechanistic understanding requires determination of the oxidation states of the crystallographically observed Fe ions in the catalytically active Fe(II)Fe(III) state, along with the site of MbnA binding. Here, we have used electron nuclear double resonance (ENDOR) spectroscopy to determine such structural and electronic properties of the active site, in particular, the mode of substrate binding to the MV state, information not accessible by X-ray crystallography alone. The oxidation states of the two Fe ions were determined by
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