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Publication Abstract from PubMed

SignificanceMethanobactins (Mbns), copper-binding peptidic compounds produced by some bacteria, are candidate therapeutics for human diseases of copper overload. The paired oxazolone-thioamide bidentate ligands of methanobactins are generated from cysteine residues in a precursor peptide, MbnA, by the MbnBC enzyme complex. MbnBC activity depends on the presence of iron and oxygen, but the catalytically active form has not been identified. Here, we provide evidence that a dinuclear Fe(II)Fe(III) center in MbnB, which is the only representative of a >13,000-member protein family to be characterized, is responsible for this reaction. These findings expand the known roles of diiron enzymes in biology and set the stage for mechanistic understanding, and ultimately engineering, of the MbnBC biosynthetic complex.

A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis.,Park YJ, Jodts RJ, Slater JW, Reyes RM, Winton VJ, Montaser RA, Thomas PM, Dowdle WB, Ruiz A, Kelleher NL, Bollinger JM Jr, Krebs C, Hoffman BM, Rosenzweig AC Proc Natl Acad Sci U S A. 2022 Mar 29;119(13):e2123566119. doi: , 10.1073/pnas.2123566119. Epub 2022 Mar 23. PMID:35320042^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.