The mitochondrial and prokaryotic proton-trans locating NADH:ubiquinone oxidoreductases:: similarities and dissimilarities of the quinone-junction sites

被引:41
作者
Grivennikova, VG
Roth, R
Zakharova, NV
Hägerhäll, C
Vinogradov, AD
机构
[1] Moscow MV Lomonosov State Univ, Sch Biol, Dept Biochem, Moscow 119992, Russia
[2] Lund Univ, Ctr Chem & Chem Engn, Dept Biochem, S-22100 Lund, Sweden
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2003年 / 1607卷 / 2-3期
关键词
NADH : ubiquinone reductase; complex; 1; NDH-1; ubiquinone; piericidin; tightly bound inhibitor; respiratory chain; bovine heart submitochondrial particle; Paracoccus denitrificans membrane; Rhodobacter capsulatus membrane;
D O I
10.1016/j.bbabio.2003.09.001
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 catalytic properties of the rotenone-sensitive NADH:ubiquinone reductase (Complex 1) in bovine heart submitochondrial particles and in inside-out vesicles derived from Paracoccus denitrificans and Rhodobacter capsulatus were compared. The prokaryotic enzymes catalyze the NADH oxidase and NADH:quinone reductase reactions with similar kinetic parameters as those for the mammalian Complex 1, except for lower apparent affinities for the substrates-nucleotides. Unidirectional competitive inhibition of NADH oxidation by ADPribose, previously discovered for submitochondrial particles, was also evident for tightly coupled R denitrificans vesicles, thus suggesting that a second, NAD(+)-specific site is present in the simpler prokaryotic enzyme. The inhibitor sensitivity of the forward and reverse electron transfer reactions was compared. In P denitrificans and Bos taurus vesicles different sensitivities to rotenone and Triton X-100 for the forward and reverse electron transfer reactions were found. In bovine heart preparations, both reactions showed the same sensitivity to piericidin, and the inhibition was titrated as a straight line. In P denitrificans, the forward and reverse reactions show different sensitivity to piericidin and the titrations of both activities were curvilinear with apparent I-50 (expressed as mole of inhibitor per mole of enzyme) independent of the enzyme concentration. This behavior is explained by a model involving two different sites rapidly interacting with piericidin within the hydrophobic phase. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:79 / 90
页数:12
相关论文
共 64 条
[21]   The transition between active and de-activated forms of NADH:: ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa [J].
Grivennikova, VG ;
Serebryanaya, DV ;
Isakova, EP ;
Belozerskaya, TA ;
Vinogradov, AD .
BIOCHEMICAL JOURNAL, 2003, 369 :619-626
[22]   Catalytic activity of NADH-ubiquinone oxidoreductase (Complex I) in intact mitochondria - Evidence for the slow active/inactive transition [J].
Grivennikova, VG ;
Kapustin, AN ;
Vinogradov, AD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (12) :9038-9044
[23]   Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition [J].
Grivennikova, VG ;
Maklashina, EO ;
Gavrikova, EV ;
Vinogradov, AD .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1997, 1319 (2-3) :223-232
[24]  
GRIVENNIKOVA VG, 2002, BBA EBEC SHORT REP, V12, P209
[25]   STUDIES ON RESPIRATORY CHAIN-LINKED REDUCED NICOTINAMIDE - ADENINE DINUCLEOTIDE DEHYDROGENASE .21. FUNCTIONAL ORGANIZATION OF RESPIRATORY CHAIN AT DEHYDROGENASE-COENZYME-Q JUNCTION [J].
GUTMAN, M ;
COLES, CJ ;
SINGER, TP ;
CASIDA, JE .
BIOCHEMISTRY, 1971, 10 (11) :2036-&
[26]  
GUTMAN M, 1970, J BIOL CHEM, V245, P1992
[27]   Complex I of Rhodobacter capsulatus and its role in reverted electron transport [J].
Herter, SM ;
Kortluke, CM ;
Drews, G .
ARCHIVES OF MICROBIOLOGY, 1998, 169 (02) :98-105
[28]  
HORGAN DJ, 1968, J BIOL CHEM, V243, P834
[29]  
HORGAN DJ, 1968, J BIOL CHEM, V243, P5967
[30]   OXIDATIVE PHOSPHORYLATION IN MICROCOCCUS DENITRIFICANS .4. FURTHER CHARACTERIZATION OF ELECTRON-TRANSFER PATHWAY AND PHOSPHORYLATION ACTIVITY IN NADH OXIDATION [J].
IMAI, K ;
ASANO, A ;
SATO, R .
JOURNAL OF BIOCHEMISTRY, 1968, 63 (02) :207-&