Research in nature reports how a B12-dependent radical enzyme carries out challenging alkylation chemistry to regulate the microbial production of methane
, Structure superimposition of substrate-free with SAH and peptide-bound with SAM structures of Mmp10., Enlargement showing the major structural movements including the α1a helix and the α1 to α4 helices of the TIM barrel. Mmp10 with peptide bound is shown in grey and without peptide in teal. Structures were aligned according to the B12 binding domain. Alignment of the peptide-bound and substrate-free SAH structures using all domains has a r.m.s.d. of 0.963 Å.
Diamonds: Reaction with 1mM Ticitrate. Squares: Reaction without Ticitrate. Circles: Control reaction without enzyme and Ticitrate. Experiments were performed in duplicate. MeCbl was detected by LC-MS analysis [M+H], Fe loop in Mmp10 . Cobalamin colored magenta, residues from Fe loop colored purple and residue from cobalamin binding domain colored teal., Cation site in Mmp10 . Na ion modelled in cation site with an average distance of 2.
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