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Biotin synthase mechanism:: on the origin of sulphur
被引:94
作者:
Bui, BTS
Florentin, D
Fournier, F
Ploux, O
Méjean, A
Marquet, A
机构:
[1] Univ Paris 06, Lab Chim Organ Biol, CNRS, UMR 7613, F-75252 Paris 05, France
[2] Univ Paris 06, Lab Chim Struct Organ & Biol, CNRS, UMR 7613, F-75252 Paris, France
关键词:
biotin synthase;
iron-sulfur cluster;
S-34 reconstituted enzyme;
sulfur donor;
D O I:
10.1016/S0014-5793(98)01464-1
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
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 mere depleted of their iron and inorganic sulphide and the resulting apoenzymes mere chemically reconstituted with FeCl3 and Na-2[S-34] to give labelled ((FeS)-S-34) enzymes. These enzymes were functional and when assayed in vitro produced labelled biotin containing about 65% of S-34. These data strongly support the hypothesis that the sulphur of biotin is derived from the (FeS) centre of the enzyme. (C) 1998 Federation of European Biochemical Societies.
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页码:226 / 230
页数:5
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