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

来源：

FEBS LETTERS | 1998年 / 440卷 / 1-2期

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.

引用

页码：226 / 230

页数：5