Proceedings of the National Academy of Sciences of the United States of America · 2022
A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis.
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Park Yun Ji, Jodts Richard J, Slater Jeffrey W, Reyes Reyvin M, Winton Valerie J, Montaser Rana A, Thomas Paul M, Dowdle William B, Ruiz Anahi, Kelleher Neil L, Bollinger J Martin, Krebs Carsten, Hoffman Brian M, Rosenzweig Amy C
Аннотация
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.