ROLE OF MULTIPLE BINDING SITES IN INHIBITION OF NADH OXIDASE BY PIERICIDIN AND ROTENONE

被引：12

作者：

GUTMAN, M

SINGER, TP

CASIDA, JE

机构：

[1] Molecular Biology Division, Veterans Administration Hospital, San Francisco

[2] Department of Biochemistry and Biophysics, University of California Medical Center, San Francisco

[3] Division of Entomology, University of California, Berkeley

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 37卷 / 04期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0006-291X(69)90854-7

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：

Scatchard plots indicate that 14C-piericidin A and -rotenone bind at 2 specific sites per mole of NADH dehydrogenase in ETP, but the titer found for complex I or mersalyl-treated ETP more closely approximates 1. The curves for inhibition of NADH oxidase by piericidin and rotenone are sigmoidal; this results from an unequal contribution of the 2 specific sites to the inhibition. An unspecific binding site also contributes to the inhibition in a manner reversed by washing the particles with bovine serum albumin (BSA). In contrast, inhibition of NADH-CoQ reductase activity is due entirely to binding at specific site(s) because BSA does not restore activity. © 1969.

引用

页码：615 / &