S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the
thioether bond in S-ribosylhomocysteine to produce L- homocysteine
and 4,5-dihydroxy-2,3-pentanedione, the precursor of type II
bacterial quorum sensing autoinducer. This work carried out
extensive mechanistic studies of the LuxS reaction. The native
metal cofactor of LuxS was identified as ferrous ion, instead of
previously reported zinc ion, with a potential catalytic role.
Substantial evidence was provided for the internal redox reaction,
which comprised two consecutive carbonyl migration steps followed
by -elimination. Three LuxS activity assays were developed and
greatly facilitated the mechanistic investigations of LuxS. Two
classes of LuxS inhibitors were designed based on metal chelation
and catalytic mechanism, respectively. They encouraged future
development of LuxS inhibitors as novel antibacterial agents and
helped probe the catalytic mechanism of LuxS.
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