First and second sphere interactions accelerate non-native N-alkylation catalysis by the thermostable, methanol-tolerant B12-dependent enzyme MtaC

The corrinoid protein MtaC, which is natively involved in methyl transferase catalysis, catalyzes N-alkylation of aniline using ethyl diazoacetate. Our results show how the native preference of B-12 scaffolds for radical versus polar chemistry translates to non-native catalysis, which could guide selection of B-12-dependent proteins for biocatalysis. MtaC also has high thermal stability and organic solvent tolerance, remaining folded even in pure methanol.

Automated summary

The corrinoid protein MtaC, originally involved in methyl transferase catalysis, can catalyze N-alkylation of aniline using ethyl diazoacetate. The study demonstrates how the specific reactivity of B-12 scaffolds for radical versus polar chemistry extends to non-native catalysis, providing guidance for selecting B-12-dependent proteins for biocatalysis. MtaC also exhibits high thermal stability and organic solvent tolerance, remaining folded even in pure methanol.