Specific orientation of porphyrin at the binding site of catalytic antibody

被引：20

作者：

KawamuraKonishi, Y ^{[1
]}

Neya, S ^{[1
]}

Funasaki, N ^{[1
]}

Suzuki, H ^{[1
]}

机构：

[1] KYOTO PHARMACEUT UNIV,DEPT CHEM PHYS,YAMASHINA,KYOTO 607,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1996年 / 225卷 / 02期

关键词：

D O I：

10.1006/bbrc.1996.1208

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：

The catalytic antibody which catalyzes insertion of a cupric ion into mesoporphyrin bound ferric N-methyl mesoporhyrin and ferric mesoporhyrin to yield the respective complexes. The binding affinity of cyanide to the ferric iron in the complexes was compared with that of free ferric porphyrins. The results indicate that the one side of the porphrin plane in the complex is thoroughly exposed to surrounding solvents and the other side interacts with the protein molecule. The cyanide binding suggests the specific orientation of distorted porphyrin at the binding site of the antibody. (C) 1996 Academic Press, Inc.

引用

页码：537 / 544

页数：8

共 14 条

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