Tritium NMR studies of the human carbonic anhydrase I-benzenesulfonamide complex

被引：12
|
作者：
Culf, AS
Gerig, JT
Williams, PG
机构：
[1] UNIV CALIF SANTA BARBARA,DEPT CHEM,SANTA BARBARA,CA 93106
[2] UNIV CALIF BERKELEY,EO LAWRENCE BERKELEY LAB,STRUCT BIOL DIV,BERKELEY,CA 94720
[3] UNIV CALIF BERKELEY,EO LAWRENCE BERKELEY LAB,NATL TRITIUM LABELLING FACIL,BERKELEY,CA 94720
来源：
JOURNAL OF BIOMOLECULAR NMR | 1997年 / 10卷 / 03期
关键词：
tritium; enzyme; carbonic anhydrase; enzyme inhibitor; aromatic ring rotation;
D O I：
10.1023/A:1018358101811
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Tritium NMR spectroscopy has been used to examine the complex formed by [4-H-3]benzenesulfon-amide and human carbonic anhydrase I. The results show that in solution the inhibitor forms a 1:1 complex with the enzyme. A 100-spin computational model of the system, constructed with reference to crystallographic results, was used to interpret tritium relaxation behavior and H-3{H-1} NOEs. The analysis shows that the rate of dissociation of the enzyme-sulfonamide complex is 0.35 s(-1) and that the aromatic ring of the inhibitor undergoes rapid rotation while complexed.
引用
收藏
页码：293 / 299
页数：7
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