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This paper provides the first in vitro evidence that the sulfur atom in biotin derives from an iron-sulfur cluster on the protein.
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This paper provides the first evidence that the active form of biotin synthase contains both a [2Fe-2S] cluster and a [4Fe-4S] cluster, and that the sulfur in biotin derives from the [2Fe-2S] cluster.
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Although the actual substrate for lipoyl synthase was incorrectly identified, this paper describes the first in vitro demonstration of lipoyl synthase activity.
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Miller J.R., Busby R.W., Jordan S.W., Cheek J., Henshaw T.F., Ashley G.W., Broderick J.B., Cronan Jr. J.E., and Marletta M.A. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 39 (2000) 15166-15178. Although the actual substrate for lipoyl synthase was incorrectly identified, this paper describes the first in vitro demonstration of lipoyl synthase activity.
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This paper describes the use of site-directed mutagenesis coupled with various analytical and spectroscopic methods to establish that MiaB contains two [4Fe-4S] clusters in its active form.
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Hernández H.L., Pierrel F., Elleingand E., García-Serres R., Huynh B.H., Johnson M.K., Fontecave M., and Atta M. MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry 46 (2007) 5140-5147. This paper describes the use of site-directed mutagenesis coupled with various analytical and spectroscopic methods to establish that MiaB contains two [4Fe-4S] clusters in its active form.
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This is an interesting paper that provides evidence that biotin synthase catalyzes multiple turnover in vivo.
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This is another interesting paper that provides evidence that proteins that are involved in iron-sulfur cluster biosynthesis are required for biotin synthase activity, suggesting that they repair the [2Fe-2S] cluster after turnover.
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Mühlenhoff U., Gerl M.J., Flauger B., Pirner H.M., Balser S., Richardt N., Lill R., and Stolz J. The iron-sulfur proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae. Eukaryot Cell 6 (2007) 495-504. This is another interesting paper that provides evidence that proteins that are involved in iron-sulfur cluster biosynthesis are required for biotin synthase activity, suggesting that they repair the [2Fe-2S] cluster after turnover.
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