Self-sacrifice in radical S-adenosylmethionine proteins |
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Authors: | Booker Squire J Cicchillo Robert M Grove Tyler L |
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Institution: | Department of Chemistry, The Pennsylvania State University, University Park, PA 16803, United States. sjb14@psu.edu |
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Abstract: | The radical SAM superfamily of metalloproteins catalyze the reductive cleavage of S-adenosyl-l-methionine to generate a 5'-deoxyadenosyl radical (5'-dA*) intermediate that is obligate for turnover. The 5'-dA* acts as a potent oxidant, initiating turnover by abstracting a hydrogen atom from an appropriate substrate. A special class of these enzymes use this strategy to functionalize unactivated C-H bonds by insertion of sulfur atoms. This review will describe the characterization of three members of this class - biotin synthase, lipoyl synthase, and MiaB protein - each of which has been shown to cannibalize itself during turnover. |
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