
The active site protonation states of perdeuterated Toho-1 β-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation
Keywords: Toho-1; Neutron diffraction; Perdeuterated neutron structure; β-Lactamase; Extended-spectrum β-lactamases; CTX-M-type ESBLs; E. coli; Escherichia coli; ESBL; extended-spectrum β-lactamases; MALDI-TOF/MS; matrix-assisted laser desorption/ionization time