EFFECT OF ETHOXYFORMIC ANHYDRIDE ON THE RIESKE IRON-SULFUR PROTEIN OF BOVINE HEART UBIQUINOL - CYTOCHROME-C OXIDOREDUCTASE

被引:13
作者
OHNISHI, T
MEINHARDT, SW
VONJAGOW, G
YAGI, T
HATEFI, Y
机构
[1] N DAKOTA STATE UNIV, DEPT BIOCHEM, FARGO, ND 58105 USA
[2] CTR BIOL CHEM, DEPT THERAPEUT BIOCHEM, FRANKFURT, GERMANY
[3] SCRIPPS RES INST, DEPT MOLEC & EXPTL MED, LA JOLLA, CA 92037 USA
关键词
ETHOXYFORMIC ANHYDRIDE(1); RIESKE IRON-SULFUR CLUSTER; EPR SPECTRA; BOVINE UBIQUINOL CYTOCHROME C OXIDOREDUCTASE; BC(1) COMPLEX; COMPLEX III;
D O I
10.1016/0014-5793(94)01021-8
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
Treatment of bovine heart ubiquinol-cytochrome c oxidoreductase (complex III, bc(1) complex) with ethocyformic anhydride (EFA) inhibits electron transfer between cytochromes b and c(1) [Yagi et al., Biochemistry 21 (1982) 4777-4782]. This paper shows that EFA alters the EPR lineshape of the Rieske iron-sulfur cluster in complex III and in the isolated Rieske protein without a significant decrease of spill concentration. The effect of EFA on the Rieske iron-sulfur cluster is competitive with that of Q(0) site inhibitors, such as stigmatellin, and is completely reversed by hydroxylamine. These results are consistent with the possible ethoxyformylation by EFA of histidine ligands of the Rieske iron-sulfur cluster at the non-iron binding imidazole nitrogens.
引用
收藏
页码:103 / 107
页数:5
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