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Literature DB >> 9862460

Biotin synthase mechanism: on the origin of sulphur.

B T Bui¹, D Florentin, F Fournier, O Ploux, A Méjean, A Marquet.

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.

Entities: Chemical Gene Species

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Year: 1998 PMID： 9862460 DOI： 10.1016/s0014-5793(98)01464-1

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

25 in total

1. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme.

Authors: Frederick Berkovitch; Yvain Nicolet; Jason T Wan; Joseph T Jarrett; Catherine L Drennan
Journal: Science Date: 2004-01-02 Impact factor: 47.728

2. Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli.

Authors: Natalia B Ugulava; Kristene K Surerus; Joseph T Jarrett
Journal: J Am Chem Soc Date: 2002-08-07 Impact factor: 15.419

3. Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion.

Authors: N B Ugulava; C J Sacanell; J T Jarrett
Journal: Biochemistry Date: 2001-07-27 Impact factor: 3.162

4. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions.

Authors: N B Ugulava; B R Gibney; J T Jarrett
Journal: Biochemistry Date: 2001-07-27 Impact factor: 3.162

Biotin synthase mechanism: on the origin of sulphur.

1. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme.

2. Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli.

3. Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion.

4. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions.

5. Role of the [2Fe-2S]2+ cluster in biotin synthase: mutagenesis of the atypical metal ligand arginine 260.

6. 9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase.

Review 7. Oxidative Cyclization in Natural Product Biosynthesis.

Review 8. Radical S-adenosylmethionine enzymes.

Review 9. Anaerobic functionalization of unactivated C-H bonds.

10. Loss of iron-sulfur clusters from biotin synthase as a result of catalysis promotes unfolding and degradation.