Zobrazeno 1 - 10
of 36
pro vyhledávání: '"A D, Sled"'
Autor:
Sergey Magnitsky, Cecilia Hägerhäll, Vladimir D. Sled, Larisa Toulokhonova, Takahiro Yano, Doshimjan S. Burbaev, Vera G. Grivennikova, Tomoko Ohnishi, Andrei D. Vinogradov
Publikováno v:
Journal of Bioenergetics and Biomembranes. 34:193-208
The proton-translocating NADH-ubiquinone oxidoreductase (complex I) is the largest and least understood respiratory complex. The intrinsic redox components (FMN and iron–sulfur clusters) reside in the promontory part of the complex. Ubiquinone is t
Autor:
Tomoko Ohnishi, Takahiro Yano, Andrei D. Vinogradov, Takao Yagi, Dosymzhan Sh. Burbaev, Vladimir D. Sled
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1365:301-308
Our recent experimental data on iron-sulfur clusters and semiquinones in the complex I segment of the respiratory chain is presented, focusing on the Paracoccus (P.) denitrificans and bovine heart studies. The iron-sulfur cluster N2 has attracted the
Publikováno v:
Journal of Biological Chemistry. 272:4201-4211
The genes encoding the proton-translocating NADH-quinone oxidoreductase (NDH-1) of a thermophilic bacterium Thermus thermophilus HB-8 were cloned and sequenced. They constitute a cluster that is composed of 14 structural genes and contains no unident
Publikováno v:
Journal of Biological Chemistry. 271:5907-5913
This study reports the expression of the flavoprotein (FP) subcomplex of the proton-translocating NADH-quinone oxidoreductase (NDH-1) from Paracoccus denitrificans, which is composed of the NQO1 (50 kDa) and the NQO2 (25 kDa) subunits. The two subuni
Autor:
Andrei D. Vinogradov, I.A. Moroz, Dosymzhan Sh. Burbaev, Vladimir D. Sled, Tomoko Ohnishi, Vera G. Grivennikova
Publikováno v:
FEBS Letters. 370:83-87
Two distinct species of Complex I-associated ubisemiquinones (SQNf and SQN,) were detected by cryogenic EPR analysis of tightly coupled submitochondrial particles oxi- dizing NADH or succinate under steady-state conditions. The g = 2.00 signals from
Publikováno v:
Journal of Biological Chemistry. 270:18264-18270
The proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans is composed of at least 14 dissimilar subunits which are designated NQO1-14 and contains one noncovalently bound FMN and at least five EPR-visible iron-sulfur cl
Publikováno v:
European Journal of Biochemistry. 230:538-548
The proton-translocating NADH:ubiquinone oxidoreductase (complex I) was isolated from Escherichia coli by chromatographic steps performed in the presence of an alkylglucoside detergent at pH 6.0. The complex is obtained in a monodisperse state with a
Publikováno v:
European Journal of Biochemistry. 230:1032-1036
The mitochondrial complex I (NADH: ubiquinone oxidoreductase) isolated from potato (Solanum tuberosum) has been investigated for the presence of iron-sulfur clusters. EPR spectroscopic analysis detected signals arising from clusters N1, N2, N3 and N4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1230:23-30
The steady-state kinetics of the NADH dehydrogenase activity of the three-subunit flavo-iron-sulfur protein (FP, Type II NADH dehydrogenase) in the presence of the one-electron acceptor hexammineruthenium(III) (HAR) were studied. The maximal catalyti
Publikováno v:
FEBS Letters. 354:160-164
In order to identify the ligand residues of the [2Fe-2S] cluster of the 25 kDa (NQO2) subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans, we mutated individually all seven cysteine residues (C61, C96, C101, C1