PMID:12148999
| Citation |
Ugulava, NB, Surerus, KK and Jarrett, JT (2002) Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli. J. Am. Chem. Soc. 124:9050-1 |
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| Abstract |
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 approximately 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. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Binding Sites; Culture Media; Escherichia coli/enzymology; Iron/chemistry; Spectroscopy, Mossbauer; Sulfides/chemistry; Sulfurtransferases/chemistry |
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