Journal
BIOCHEMISTRY
Volume 55, Issue 39, Pages 5531-5536Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00670
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Funding
- National Institutes of Health [GM-101957, GM-120283]
- Howard Hughes Medical Institute
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The methylthiotransferases (MTTases) represent a subfamily of the S-adenosylmethionine (AdoMet) radical superfamily of enzymes that catalyze the attachment of a methylthioether (-SCH3) moiety on unactivated carbon centers. These enzymes contain two, [4Fe-4S] clusters, one of which participates in the reductive fragmention of AdoMet to generate a 5'-deoxyadenosyl 5'-radical and the other of which, termed the auxiliary cluster, is believed to play a central role in constructing the methylthio group and attaching, it to the substrate. Because the redox properties of the bound cofactors within the AdoMet radical superfamily are so poorly understood, we have examined two MTTases in parallel, MiaB and RimO, using, protein, electrochemistry. We resolve the redox potentials of each [4Fe-4S] cluster, show that the auxiliary duster has a potential higher than-that of the AdoMet-binding cluster, and demonstrate that upon incubation of either enzyme with AdoMet, a unique low-potential state of the enzyme emerges. Our results are consistent with a mechanism whereby the auxiliary cluster is transiently methylated during substrate methylthiolation.
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