A MODEL FOR THE INTERACTION OF ALCOHOL WITH THE ZINC THIOLATE SITE OFALCOHOL-DEHYDROGENASE

Authors
SHONER SC HUMPHREYS KJ BARNHART D KOVACS JA
Citation
Sc. Shoner et al., A MODEL FOR THE INTERACTION OF ALCOHOL WITH THE ZINC THIOLATE SITE OFALCOHOL-DEHYDROGENASE, Inorganic chemistry, 34(24), 1995, pp. 5933
Citations number
33
Categorie Soggetti
Chemistry Inorganic & Nuclear
Journal title
Inorganic chemistry → ACNP
ISSN journal
00201669
Volume
34
Issue
24
Year of publication
1995
Database
ISI
SICI code
0020-1669(1995)34:24<5933:AMFTIO>2.0.ZU;2-C
Abstract
Two thiolate-ligated zinc complexes, ZnL(S3(Me)N3)(Pr)(.-)MeOH (1) and hydride-reduced ZnL(S2(Me)N3(Pr)H4)(.-)MeOH (2), are reported, each c ontaining a cocrystallized MeOH molecule H-bonded to a zinc-bound sulf ur. IR and X-ray structural data indicate that the S ... H-OMe interac tion in 2 is comparable to the interaction between Et(3)N and H-OMe. T hese data suggest that, in liver alcohol dehydrogenase, alcohols may b e activated in a similar manner, without requiring prior coordination to the metal.