V. Sled'

发表

Characterization of the chloroplast cytochrome b6f complex as a structural and functional dimer.

H. Schägger, T. Baker, R. Cheng, 1994, Biochemistry.

Disruption of the gene encoding the NADH-binding subunit of NADH: ubiquinone oxidoreductase in Neurospora crassa. Formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3.

T. Ohnishi, H. Weiss, W. Fecke, 1994, European journal of biochemistry.

Ubisemiquinone in the NADH‐ubiquinone reductase region of the mitochondrial respiratory chain

I. A. Moroz, A. Vinogradov, A. Kotlyar, 1989 .

The amino-terminal portion of the Rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex.

F. Daldal, G. Brasseur, U. Liebl, 1997, Biochemistry.

The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate:menaquinone reductase; effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties.

L. Hederstedt, T. Ohnishi, C. Hägerhäll, 1995, Biochimica et biophysica acta.

Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain.

T. Yagi, A. Vinogradov, T. Ohnishi, 1998, Biochimica et biophysica acta.

Expression and Characterization of the Flavoprotein Subcomplex Composed of 50-kDa (NQO1) and 25-kDa (NQO2) Subunits of the Proton-translocating NADH-Quinone Oxidoreductase of Paracoccus denitrificans(*)

T. Yagi, T. Ohnishi, T. Yano, 1996, The Journal of Biological Chemistry.

Reductive inactivation of the mitochondrial three subunit NADH dehydrogenase.

A. Vinogradov, V. Sled', 1993, Biochimica et biophysica acta.

Kinetics of the mitochondrial NADH-ubiquinone oxidoreductase interaction with hexammineruthenium(III).

A. Vinogradov, V. Sled', 1993, Biochimica et biophysica acta.

Coupling site I and the rotenone‐sensitive ubisemiquinone in tightly coupled submitochondrial particles

I. A. Moroz, A. Vinogradov, A. Kotlyar, 1990, FEBS letters.

Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems

R. Gennis, T. Friedrich, T. Ohnishi, 1993, Journal of bioenergetics and biomembranes.

Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli.

T. Friedrich, T. Ohnishi, H. Weiss, 1995, European journal of biochemistry.

A reductant-induced oxidation mechanism for complex I.

P. Dutton, F. Daldal, T. Ohnishi, 1998, Biochimica et biophysica acta.

EPR Characterization of Ubisemiquinones and Iron–Sulfur Cluster N2, Central Components of the Energy Coupling in the NADH-Ubiquinone Oxidoreductase (Complex I) In Situ

A. Vinogradov, V. G. Grivennikova, T. Ohnishi, 2002, Journal of bioenergetics and biomembranes.

Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I).

Y. Hatefi, T. Ohnishi, T Ohnishi, 1994, Biochemistry.

Kinetics of the mitochondrial three-subunit NADH dehydrogenase interaction with hexammineruthenium(III).

A. Vinogradov, V. G. Grivennikova, T. Ohnishi, 1995, Biochimica et biophysica acta.

The Proton-translocating NADH-Quinone Oxidoreductase (NDH-1) of Thermophilic Bacterium Thermus thermophilus HB-8

T. Yagi, T. Ohnishi, T. Yano, 1997, The Journal of Biological Chemistry.

Characterization of the Putative 2×[4Fe-4S]-binding NQO9 Subunit of the Proton-translocating NADH-Quinone Oxidoreductase (NDH-1) of Paracoccus denitrificans

T. Yagi, T. Ohnishi, T. Yano, 1999, The Journal of Biological Chemistry.

Analysis of the iron-sulfur clusters within the complex I (NADH:ubiquinone oxidoreductase) isolated from potato tuber mitochondria.

A. Brennicke, T. Ohnishi, L. Grohmann, 1995, European journal of biochemistry.

Expression and Characterization of the 66-Kilodalton (NQO3) Iron-Sulfur Subunit of the Proton-translocating NADH-Quinone Oxidoreductase of Paracoccus denitrificans(*)

T. Yagi, T. Ohnishi, T. Yano, 1995, The Journal of Biological Chemistry.

Identification of amino acid residues associated with the [2Fe‐2S] cluster of the 25 kDa (NQO2) subunit of the proton‐translocating NADH‐quinone oxidoreductase of Paracoccus denitrificans

T. Yagi, T. Ohnishi, T. Yano, 1994, FEBS letters.

Effect of Ca2+ ions on the slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase.

A. Vinogradov, A. Kotlyar, V. Sled', 1992, Biochimica et biophysica acta.

Expression of the 25-kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans.

T. Yagi, T. Ohnishi, T. Yano, 1994, Biochemistry.

HYSTERESIS IN THE BEHAVIOR OF BOVINE HEART MITOCHONDRIAL COMPLEX I : KINETIC AND THERMODYNAMIC PARAMETERS OF THE SLOW REVERSIBLE ACTIVE/INACTIVE TRANS ITION

A. Vinogradov, E. Maklashina, V. Sled', 1994 .

[Hysteresis behavior of complex I from bovine heart mitochondria: kinetic and thermodynamic parameters of retarded reverse transition from the inactive to active state].

A. Vinogradov, E. Maklashina, V. Sled', 1994, Biokhimiia.

Conserved Non Liganding Residues of Rhodobacter (R.) Capsulatus ‘Rieske’ Protein are Essential for [2Fe-2S] Cluster Properties and Communication with the Quinone Pool

F. Daldal, U. Liebl, T. Ohnishi, 1995 .

Conserved nonliganding residues of the Rhodobacter capsulatus Rieske iron-sulfur protein of the bc1 complex are essential for protein structure, properties of the [2Fe-2S] cluster, and communication with the quinone pool.

F. Daldal, G. Brasseur, U. Liebl, 1997, Biochemistry.

Characterization and Crystallization of the Lumen Side Domain of the Chloroplast Rieske Iron-Sulfur Protein*

Janet L. Smith, C. Carrell, W. Cramer, 1996, The Journal of Biological Chemistry.

Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli.

T. Friedrich, T. Ohnishi, H. Weiss, 1995, European journal of biochemistry.

Topographical distribution of redox centres and the Qo site in ubiquinol-cytochrome-c oxidoreductase (complex III) and ligand structure of the Rieske iron-sulphur cluster.

F. Daldal, T. Yagi, Y. Hatefi, 1994, Biochemical Society Transactions.

An Escherichia coli Mutant Quinol:Fumarate Reductase Contains an EPR-detectable Semiquinone Stabilized at the Proximal Quinone-binding Site*

R. Gunsalus, I. Schröder, G. Cecchini, 1999, The Journal of Biological Chemistry.