Biotin synthase mechanism: on the origin of sulphur

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Abstract

Biotin synthase catalyses the last step of the biosynthesis of biotin in microorganisms and plants. The active protein isolated from Bacillus sphaericus and Escherichia coli contains an iron-sulphur (FeS) cluster. The native enzymes were depleted of their iron and inorganic sulphide and the resulting apoenzymes were chemically reconstituted with FeCl3 and Na2[34S] to give labelled (Fe34S) enzymes. These enzymes were functional and when assayed in vitro produced labelled biotin containing about 65% of 34S. These data strongly support the hypothesis that the sulphur of biotin is derived from the (FeS) centre of the enzyme. Copyright (C) 1998 Federation of European Biochemical Societies.

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Tse Sum Bui, B., Florentin, D., Fournier, F., Ploux, O., Méjean, A., & Marquet, A. (1998). Biotin synthase mechanism: on the origin of sulphur. FEBS Letters, 440(1–2), 226–230. https://doi.org/10.1016/S0014-5793(98)01464-1

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