ANTIOXIDANT EFFECT OF COENZYME-Q ON HYDROGEN PEROXIDE-ACTIVATED MYOGLOBIN

被引:0
作者
MORDENTE, A
MARTORANA, GE
SANTINI, SA
MIGGIANO, GAD
PETITTI, T
GIARDINA, B
BATTINO, M
LITTARRU, GP
机构
[1] UNIV ANCONA, IST BIOCHIM, I-60100 ANCONA, ITALY
[2] UNIV CATTOLICA SACRO CUORE, IST CHIM, I-00168 ROME, ITALY
来源
CLINICAL INVESTIGATOR | 1993年 / 71卷 / 08期
关键词
UBIQUINOL; ANTIOXIDANT; FERRYLMYOGLOBIN; OXIDATIVE STRESS;
D O I
暂无
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
In recent years increased attention has been focused on the reduced forms of coenzyme Q as antioxidant compounds inhibiting lipid peroxidation in model systems and in biological membranes, but in spite of extensive experimental evidences the molecular mechanisms responsible for the antioxidant activity of ubiquinones are still debated. Ferrylmyoglobin and/or its free radical form are regarded as powerful oxidizing agents capable of promoting oxidation of essential cellular constituents, particularly cell membranes. Therefore, we investigated the effects of ubiquinol on the formation and survival of ferryl species of myoglobin and on metmyoglobin itself. The addition of a threefold molar excess of hydrogen peroxide to a solution of metmyoglobin induces the rapid formation of a compound with the spectral characteristics of ferrylmyoglobin. The reaction is complete within 4 min, producing up to 76% of ferrylmyoglobin, which remains stable for at least 30 min. The addition of ubiquinol-1 to the same solution provokes a rapid and progressive reduction of ferrylmyoglobin to metmyoglobin and oxymyoglobin. Ubiquinol-1, furthermore, is also capable of protecting metmyoglobin against oxidation when added in the solution before hydrogen peroxide. Ubiquinol-1, indeed, is effective at both limiting the maximal ferrylmyoglobin level attained (59% inhibition) and accomplishing complete removal of the ferryl form (in about 15 min). The results demonstrate that ubiquinol is capable of reducing both ferrylmyoglobin and metmyoglobin to oxymyoglobin, providing a novel antioxidant mechanism for coenzyme Q.
引用
收藏
页码:S92 / S96
页数:5
相关论文
共 18 条
[1]   THE REDUCTION OF FERRYL MYOGLOBIN BY ERGOTHIONEINE - A NOVEL FUNCTION FOR ERGOTHIONEINE [J].
ARDUINI, A ;
EDDY, L ;
HOCHSTEIN, P .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1990, 281 (01) :41-43
[2]   THE PARTICIPATION OF COENZYME-Q IN FREE-RADICAL PRODUCTION AND ANTIOXIDATION [J].
BEYER, RE .
FREE RADICAL BIOLOGY AND MEDICINE, 1990, 8 (06) :545-565
[3]   REDUCTION OF FERRYLMYOGLOBIN TO METMYOGLOBIN BY QUINONOID COMPOUNDS [J].
BUFFINTON, G ;
CADENAS, E .
CHEMICO-BIOLOGICAL INTERACTIONS, 1988, 66 (3-4) :233-250
[4]   UBIQUINOL-10 IS AN EFFECTIVE LIPID-SOLUBLE ANTIOXIDANT AT PHYSIOLOGICAL CONCENTRATIONS [J].
FREI, B ;
KIM, MC ;
AMES, BN .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (12) :4879-4883
[5]   REDOX CYCLING OF MYOGLOBIN AND ASCORBATE - A POTENTIAL PROTECTIVE MECHANISM AGAINST OXIDATIVE REPERFUSION INJURY IN MUSCLE [J].
GALARIS, D ;
CADENAS, E ;
HOCHSTEIN, P .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1989, 273 (02) :497-504
[6]   MECHANISMS OF REOXYGENATION INJURY IN MYOCARDIAL-INFARCTION - IMPLICATIONS OF A MYOGLOBIN REDOX CYCLE [J].
GALARIS, D ;
EDDY, L ;
ARDUINI, A ;
CADENAS, E ;
HOCHSTEIN, P .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 160 (03) :1162-1168
[7]   GLUTATHIONE-DEPENDENT REDUCTION OF PEROXIDES DURING FERRYL-MYOGLOBIN AND MET-MYOGLOBIN INTERCONVERSION - A POTENTIAL PROTECTIVE MECHANISM IN MUSCLE [J].
GALARIS, D ;
CADENAS, E ;
HOCHSTEIN, P .
FREE RADICAL BIOLOGY AND MEDICINE, 1989, 6 (05) :473-478
[8]   THE 2-ELECTRON REDUCTION OF SPERM WHALE FERRYL MYOGLOBIN BY ETHANOL [J].
HARADA, K ;
TAMURA, M ;
YAMAZAKI, I .
JOURNAL OF BIOCHEMISTRY, 1986, 100 (02) :499-504
[9]   ANTIOXIDANT ACTION OF UBIQUINOL HOMOLOGS WITH DIFFERENT ISOPRENOID CHAIN-LENGTH IN BIOMEMBRANES [J].
KAGAN, VE ;
SERBINOVA, EA ;
KOYNOVA, GM ;
KITANOVA, SA ;
TYURIN, VA ;
STOYTCHEV, TS ;
QUINN, PJ ;
PACKER, L .
FREE RADICAL BIOLOGY AND MEDICINE, 1990, 9 (02) :117-126
[10]   LIPID-PEROXIDATION AND OXIDATION OF SEVERAL COMPOUNDS BY H2O2 ACTIVATED METMYOGLOBIN [J].
KANNER, J ;
HAREL, S .
LIPIDS, 1985, 20 (09) :625-628