Methylation of (2-methylethanethiol-bis-3,5-dimethylpyrazolyl)methane zinccomplexes and coordination of the resulting thioether: Relevance to zinc-containing alkyl transfer enzymes
Bs. Hammes et Cj. Carrano, Methylation of (2-methylethanethiol-bis-3,5-dimethylpyrazolyl)methane zinccomplexes and coordination of the resulting thioether: Relevance to zinc-containing alkyl transfer enzymes, INORG CHEM, 40(5), 2001, pp. 919-927
A series of zinc complexes using a new tripodal, N2S, heteroscorpionate lig
and (L3SH) that is isostructural and isoelectronic with the well-known N-3
trispyrazolylborates have been methylated in solution and the coordination
properties of the resulting thioether examined. This system models the reac
tivity of zinc-containing enzymes involved in alkyl group transfers such as
the DNA repair protein Ada from E. coli, or farnasyl transferase where it
has been shown that the thioether resulting from alkyl group transfer remai
ns in the coordination sphere of the zinc. The following complexes have bee
n structurally characterized: [(L3S)ZnI] (1), [(L3SCH(3))ZnI2] (2), [(L3SCH
(3))ZnI]BF4 (3), [(L3SCH(3))Zn-mu -bis-acetato-mu -hydroxo-Zn(L3SCH(3))]BF4
(5), [(L3SCH(3))ZnSPhF5]ClO4 (7), and [(L3SCH(3))(2)Zn](BF4)(2) (8). Compl
exes 3, 4, 5, 7. and 8 all display thioether coordination. Thus in the abse
nce of superior anionic ligands, thioethers are reasonably good donors to z
inc in either a tetrahedral or octahedral geometry. The methylation of the
complex [(L3S)ZnSPhF5], which contains two different thiols, produces a sin
gle product, 7, where only the aliphatic thiol has been alkylated. This obs
ervation validates the suggestion that reactivity in enzymes with multiple
zinc-bound thiols could be controlled by differences in thiol pK(a) (Hammes
, B. S.; Warthen, C. R.; Crans, D.; Carrano, C. J. J. Biol. Inorg. Chern. 2
000, 6, 82. Compound 7 is also of interest in that it resembles the metal i
on-binding site of the blue copper protein, azurin.