PMID:9862460
| Citation |
Bui, BT, Florentin, D, Fournier, F, Ploux, O, Méjean, A and Marquet, A (1998) Biotin synthase mechanism: on the origin of sulphur. FEBS Lett. 440:226-30 |
|---|---|
| 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. |
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| Keywords |
Apoenzymes/metabolism; Bacillus/enzymology; Bacillus/metabolism; Bacterial Proteins/metabolism; Biotin/biosynthesis; Biotin/chemistry; Chlorides; Escherichia coli/enzymology; Escherichia coli/metabolism; Ferric Compounds/metabolism; Holoenzymes/metabolism; Iron/metabolism; Kinetics; Mass Spectrometry; Models, Chemical; Sulfides/metabolism; Sulfur/metabolism; Sulfurtransferases/chemistry; Sulfurtransferases/metabolism |
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