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

被引:27
|
作者
SHONER, SC [1 ]
HUMPHREYS, KJ [1 ]
BARNHART, D [1 ]
KOVACS, JA [1 ]
机构
[1] UNIV WASHINGTON,DEPT CHEM,SEATTLE,WA 98195
关键词
D O I
10.1021/ic00128a002
中图分类号
O61 [无机化学];
学科分类号
070301 ; 081704 ;
摘要
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 containing a cocrystallized MeOH molecule H-bonded to a zinc-bound sulfur. IR and X-ray structural data indicate that the S ... H-OMe interaction in 2 is comparable to the interaction between Et(3)N and H-OMe. These data suggest that, in liver alcohol dehydrogenase, alcohols may be activated in a similar manner, without requiring prior coordination to the metal.
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页码:5933 / &
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