Our work on the MoaC mechanism was published in ACS Biochemistry

This paper describes successful entrapment of previously uncharacterized reaction intermediate of MoaC reaction using an uncleavable substrate analog, 3′,8-cH2GTP.  Intriguingly, the trapped intermediate was tightly bound to MoaC, likely through covalent modification, making the analog as the first mechanism-based inhibitor of bacterial Moco biosynthesis.  The results revealed that the unique tetracyclic structure of cPMP (MoaC product) was constructed via a concerted formation of pterin and cyclic phosphate rings, which is distinct from previously proposed stepwise mechanism.  Brad found the irreversible inhibition and performed most of the basic characterization, and Edward performed some nice follow up experiments including the MS characterization of the inhibited MoaC.

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