THE OXIDATION OF CYTOCHROME-C-OXIDASE VESICLES BY HEMOGLOBIN

被引：20

作者：

SARTI, P

HOGG, N

DARLEYUSMAR, VM

SANNA, MT

WILSON, MT

机构：

[1] UNIV ESSEX, COLCHESTER CO4 3SQ, ESSEX, ENGLAND

[2] CNR, CTR MOLEC BIOL, I-00185 ROME, ITALY

[3] UNIV CAGLIARI, INST BIOL CHEM, I-09100 CAGLIARI, ITALY

[4] WELLCOME RES LABS, BECKENHAM BR3 3BS, KENT, ENGLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1994年 / 1208卷 / 01期

关键词：

MEMBRANE OXIDATION; HEMOPROTEINS; CYTOCHROME-C OXIDASE; PEROXYL RADICAL; LIPOSOME;

D O I：

10.1016/0167-4838(94)90157-0

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：

Human hemoglobin has been used as a pro-oxidant for artificial unilamellar phospholipid vesicles, containing cytochrome-c oxidase inserted into the bilayer. This experimental system was suitable to follow directly the kinetics of lipid oxidation and the effects on both the vesicle membrane permeability and the functional state of cytochrome-c oxidase. Following mixing of vesicles with hemoglobin, an oxygen dependent, peroxyl radical mediated, rapid oxidation (taking a few minutes) of the lipid was found to occur. On a similar time scale the membrane became ion-leaky and cytochrome-c oxidase damaged. The pro-oxidant effects of hemoglobin in various oxidation and ligation states were studied and a mechanism, based on a ferric/ferryl redox cycle of the heme-iron is proposed to account for these observations.

引用

页码：38 / 44

页数：7

共 28 条

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[2]

ANTONINI G, 1991, J BIOL CHEM, V266, P13193

[3] CYTOCHROME-C OXIDASE BINDING OF HYDROGEN-PEROXIDE [J].