Cherimolin-1, new selective inhibitor of the first energy-coupling site of the NADH:ubiquinone oxidoreductase (complex I)

被引:22
作者
Estornell, E [1 ]
Tormo, JR [1 ]
Cortes, D [1 ]
机构
[1] UNIV VALENCIA,FAC FARM,DEPT FARMACOL FARMACOGNOSIA & FARMACODINAMIA,E-46100 BURJASSOT,VALENCIA,SPAIN
关键词
D O I
10.1006/bbrc.1997.7637
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 mechanism linking electron transport to proton translocation in the NADH:ubiquinone oxidoreductase (complex I of the mitochondrial respiratory chain) is still unclear. Inhibitors acting at different sites of the enzyme are powerful tools to clarify this mechanism. Up to now, a unique inhibitor, the Annonaceous acetogenin rolliniastatin-2, selectively blocks the most internal proton-translocation site. This study introduces cherimolin-1, a new acetogenin that inhibits the complex I with this special mode of action, which is more easily available from the plant material. Moreover, the mode of action of this scarce type of complex I inhibitor is further characterized. (C) 1997 Academic Press.
引用
收藏
页码:234 / 238
页数:5
相关论文
共 31 条
[21]   Proton pumping of mitochondrial complex I: Differential activation by analogs of ubiquinone [J].
Helfenbaum, L ;
Ngo, A ;
Ghelli, A ;
Linnane, AW ;
Esposti, MD .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1997, 29 (01) :71-80
[22]   Quinolones and their n-oxides as inhibitors of mitochondrial complexes I and III [J].
Reil, E ;
Hofle, G ;
Draber, W ;
Oettmeier, W .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1997, 1318 (1-2) :291-298
[23]   Comparison of the structural features of ubiquinone reduction sites between glucose dehydrogenase in Escherichia coli and bovine heart mitochondrial complex I [J].
Sakamoto, K ;
Miyoshi, H ;
Matsushita, K ;
Nakagawa, M ;
Ikeda, J ;
Ohshima, M ;
Adachi, O ;
Akagi, T ;
Iwamura, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 237 (01) :128-135
[24]  
SINGER TP, 1994, BIOCHIM BIOPHYS ACTA, V1187, P18
[25]   Structural studies of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: Identity, property, and stoichiometry of the peripheral subunits [J].
Takano, S ;
Yano, T ;
Yagi, T .
BIOCHEMISTRY, 1996, 35 (28) :9120-9127
[26]   Structural factors of rotenone required for inhibition of various NADH-ubiquinone oxidoreductases [J].
Ueno, H ;
Miyoshi, H ;
Inoue, M ;
Niidome, Y ;
Iwamura, H .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1996, 1276 (03) :195-202
[27]   KINETICS, CONTROL, AND MECHANISM OF UBIQUINONE REDUCTION BY THE MAMMALIAN RESPIRATORY CHAIN-LINKED NADH-UBIQUINONE REDUCTASE [J].
VINOGRADOV, AD .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1993, 25 (04) :367-375
[28]   THE NADH - UBIQUINONE OXIDOREDUCTASE (COMPLEX-I) OF RESPIRATORY CHAINS [J].
WALKER, JE .
QUARTERLY REVIEWS OF BIOPHYSICS, 1992, 25 (03) :253-324
[29]   THE RESPIRATORY-CHAIN NADH DEHYDROGENASE (COMPLEX-I) OF MITOCHONDRIA [J].
WEISS, H ;
FRIEDRICH, T ;
HOFHAUS, G ;
PREIS, D .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 197 (03) :563-576
[30]   The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8 - Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQ02 subunit [J].
Yano, T ;
Chu, SS ;
Sled, VD ;
Ohnishi, T ;
Yagi, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (07) :4201-4211