FEBS Letters | |
Biotin synthase mechanism: on the origin of sulphur | |
Méjean, Annick2  Fournier, Françoise1  Tse Sum Bui, Bernadette2  Florentin, Dominique2  Marquet, Andrée2  Ploux, Olivier2  | |
[1] Laboratoire de Chimie Structurale Organique et Biologique, Université Paris VI – CNRS UMR 7613, 4 place Jussieu, 75252 Paris Cedex 05, France;Laboratoire de Chimie Organique Biologique, Université Paris VI – CNRS UMR 7613, 4 place Jussieu, 75252 Paris Cedex 05, France | |
关键词: Biotin synthase; Iron-sulfur cluster; 34S reconstituted enzyme; Sulfur donor; (FeS); iron-sulphur cluster; AdoMet; S-adenosylmethionine; DTT; dithiothreitol; DTB; dethiobiotin; Ado-CH2 ⋅; deoxyadenosyl radical; PFL; pyruvate formate lyase; ARNR; anaerobic ribonucleotide reductase; LAM; lysine 2; 3-aminomutase; | |
DOI : 10.1016/S0014-5793(98)01464-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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