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

被引:59
作者
Ugulava, NB
Surerus, KK
Jarrett, JT [1 ]
机构
[1] Univ Penn, Johnson Res Fdn, Philadelphia, PA 19104 USA
[2] Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA
[3] Univ Wisconsin, Dept Chem, Milwaukee, WI 53201 USA
关键词
D O I
10.1021/ja027004j
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Biotin synthase is an AdoMet-dependent radical enzyme that catalyzes the insertion of an FeS cluster-derived sulfur atom into dethiobiotin. The dimeric enzyme is purified containing one [2Fe-2S]2+ cluster per monomer, but it is most active when reconstituted with an additional [4Fe-4S]2+ cluster per monomer. Using Mössbauer spectroscopy coupled with differential reconstitution of each cluster with 57Fe, we show that the reconstituted enzyme has ∼1:1 [2Fe-2S]2+ and [4Fe-4S]2+ clusters and that the [4Fe-4S]2+ cluster is assembled at an alternate site not previously occupied by the [2Fe-2S]2+ cluster. These data suggest that biotin synthase is evolved to simultaneously accommodate two different clusters with unique roles in catalysis. Copyright © 2002 American Chemical Society.
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页码:9050 / 9051
页数:2
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