Front Cover: Structures in Tetrahydrofolate Methylation in Desulfitobacterial Glycine Betaine Metabolism at Atomic Resolution (ChemBioChem 6/2020)

Enzymes that orchestrate methylation between tetrahydrofolate (THF) and cobalamin are abundant among all domains of life. During the energy‐producing catabolism of glycine betaine in Desulfitobacterium hafniense , MtgA catalyzes methyl transfer from methylcobalamin to THF. Atomic insights into the substrate–enzyme interactions of MtgA and THF as well as analysis of a trapped (THF‐CH 3 ) + reaction intermediate in sp 3 hybridization reveal a unique binding mode for the THF glutamyl‐ p ‐aminobenzoate moiety during methyl transfer. More information can be found in the communication by M. Groll and T. Badmann on page 776 in Issue 6, 2020 (DOI: 10.1002/cbic.201900515).