A. Vinogradov

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NADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I).

A. Vinogradov, 2008, Biochimica et biophysica acta.

Catalytic Activity of NADH-ubiquinone Oxidoreductase (Complex I) in Intact Mitochondria

A. Vinogradov, V. G. Grivennikova, A. Kapustin, 2001, The Journal of Biological Chemistry.

In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria.

A. Vinogradov, V. G. Grivennikova, I. Gostimskaya, 2003, Analytical biochemistry.

Mitochondrial hydrogen peroxide production as determined by the pyridine nucleotide pool and its redox state.

A. Vinogradov, V. G. Grivennikova, Alexandra V. Kareyeva, 2012, Biochimica et biophysica acta.

Energy‐dependent transformation of the catalytic activities of the mitochondrial F0·F1‐ATP synthase

A. Vinogradov, M. Galkin, 1999, FEBS letters.

Triton X-100 as a specific inhibitor of the mammalian NADH-ubiquinone oxidoreductase (Complex I).

A. Vinogradov, V. G. Grivennikova, T. Ohnishi, 1999, Biochimica et biophysica acta.

ATPase/synthase activity of Paracoccus denitrificans Fo·F1 as related to the respiratory control phenomenon.

A. Vinogradov, T. V. Zharova, 2014, Biochimica et biophysica acta.

Molecular identification of the enzyme responsible for the mitochondrial NADH‐supported ammonium‐dependent hydrogen peroxide production

G. Cecchini, A. Vinogradov, V. G. Grivennikova, 2011, FEBS letters.

Generation of superoxide by the mitochondrial Complex I.

A. Vinogradov, V. G. Grivennikova, 2006, Biochimica et biophysica acta.

Ammonium‐dependent hydrogen peroxide production by mitochondria

G. Cecchini, A. Vinogradov, V. G. Grivennikova, 2008, FEBS letters.

Oxygen-dependence of mitochondrial ROS production as detected by Amplex Red assay

A. Vinogradov, V. G. Grivennikova, Alexandra V. Kareyeva, 2018, Redox biology.

Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition.

A. Vinogradov, V. G. Grivennikova, E. Maklashina, 1997, Biochimica et biophysica acta.

[37] The keilin-hartree heart muscle preparation

A. Vinogradov, T. King, 1979 .

The Keilin-Hartree heart muscle preparation.

A. Vinogradov, T. King, 1979, Methods in enzymology.

Identification of the Mitochondrial ND3 Subunit as a Structural Component Involved in the Active/Deactive Enzyme Transition of Respiratory Complex I*

H. Schägger, M. Karas, I. Wittig, 2008, Journal of Biological Chemistry.

Generation of superoxide-radical by the NADH: Ubiquinone oxidoreductase of heart mitochondria

A. Vinogradov, V. G. Grivennikova, 2005, Biochemistry (Moscow).

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

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

Energy-linked binding of Pi is required for continuous steady-state proton-translocating ATP hydrolysis catalyzed by F0.F1 ATP synthase.

A. Vinogradov, T. V. Zharova, 2006, Biochemistry.

Requirement of medium ADP for the steady-state hydrolysis of ATP by the proton-translocating Paracoccus denitrificans Fo.F1-ATP synthase.

A. Vinogradov, T. V. Zharova, 2006, Biochimica et biophysica acta.

Paracoccus denitrificans proton-translocating ATPase: Kinetics of oxidative phosphorylation

A. Vinogradov, T. V. Zharova, K. A. Kegyarikova, 2010, Biochemistry (Moscow).

Nucleotide/H+‐dependent change in Mg2+ affinity at the ATPase inhibitory site of the mitochondrial F1‐F0 ATP synthase

V. V. Bulygin, A. Vinogradov, A. Syroeshkin, 1993, FEBS letters.

Inhibitory effect of palmitate on the mitochondrial NADH:ubiquinone oxidoreductase (complex I) as related to the active-de-active enzyme transition.

G. Cecchini, A. Vinogradov, V. G. Grivennikova, 2005, The Biochemical journal.

Mg2+-induced ADP-dependent inhibition of the ATPase activity of beef heart mitochondrial coupling factor F1.

A. Vinogradov, I. Minkov, A. F. Fitin, 1979, Biochemical and biophysical research communications.

An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles.

A. Vinogradov, A. F. Fitin, E. Vasilyeva, 1979, Biochemical and biophysical research communications.

Calcium and pyridine nucleotide interaction in mitochondrial membranes.

B. Chance, A. Vinogradov, A. Scarpa, 1972, Archives of biochemistry and biophysics.

Fluorescence of nicotinamide adenine dinucleotides during the active transport of Ca2+ ions in liver mitochondria

A. Vinogradov, J. N. Leikin, 1972, Journal of bioenergetics.

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.

An increase of the energy coupling capacity of submitochondrial particles by lanthanides

A. Vinogradov, V. G. Grivennikova, E. V. Gavrikova, 1994, FEBS letters.

Synergetic inhibition of the brain mitochondrial NADH: Ubiquinone oxidoreductase (Complex I) by fatty acids and Ca2+

A. Vinogradov, V. G. Grivennikova, D. S. Kalashnikov, 2011, Biochemistry (Moscow).

Submitochondrial fragments of brain mitochondria: General characteristics and catalytic properties of NADH:ubiquinone oxidoreductase (Complex I)

A. Vinogradov, V. G. Grivennikova, D. S. Kalashnikov, 2011, Biochemistry (Moscow).

$$\vec H^ + /2\bar e $$ Stoichiometry of the NADH:Ubiquinone Reductase Reaction Catalyzed by Submitochondrial Particles

A. Vinogradov, V. G. Grivennikova, A. Galkin, 2001, Biochemistry (Moscow).

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

N. Zakharova, A. Vinogradov, V. G. Grivennikova, 2003, Biochimica et biophysica acta.

The transition between active and de-activated forms of NADH:ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa.

A. Vinogradov, V. G. Grivennikova, E. Isakova, 2003, The Biochemical journal.

A competitive inhibition of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) by ADP-ribose.

A. Vinogradov, T. V. Zharova, 1997, Biochimica et biophysica acta.

Slow Ca2+‐induced inactive/active transition of the energy‐dependent Ca2+ transporting system of rat liver mitochondria: clue for Ca2+ influx cooperativity

A. Vinogradov, F. Kasparinsky, F.O. Kasparinsky, 1996, FEBS letters.

An increase in the energy coupling capacity of submitochondrial particles in the presence of lanthanides

A. Vinogradov, V. G. Grivennikova, E. V. Gavrikova, 1994, FEBS letters.

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.

Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase.

A. Vinogradov, A. Kotlyar, 1990, 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.

Isolation and properties of oxaloacetate keto-enol-tautomerases from bovine heart mitochondria.

V. I. Burov, A. Vinogradov, Y. Belikova, 1988, Biochimica et biophysica acta.

Studies on the succinate dehydrogenating system. Interaction of the mitochondrial succinate-ubiquinone reductase with pyridoxal phosphate.

A. Vinogradov, A. Kotlyar, Z. Choudhry, 1986, Biochimica et biophysica acta.

Pyridoxal phosphate‐induced dissociation of the succinate : ubiquinone reductase

A. Vinogradov, A. Kotlyar, E. V. Gavrikova, 1985, FEBS letters.

Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitors.

A. Vinogradov, A. Kotlyar, 1984, Biochimica et Biophysica Acta.

Sulphate ion-induced slow transformation of succinate dehydrogenase.

A. Vinogradov, A. Kotlyar, 1983, Biochimica et biophysica acta.

Kinetics of ubiquinone reduction by the resolved succinate: ubiquinone reductase.

A. Vinogradov, V. G. Grivennikova, 1982, Biochimica et biophysica acta.

Fumarate reductase activity of bovine heart succinate-ubiquinone reductase. New assay system and overall properties of the reaction.

A. Vinogradov, A. Timoshin, V. G. Grivennikova, 1993, Biochimica et biophysica acta.

Studies on the succinate dehydrogenating system. Isolation and properties of the mitochondrial succinate-ubiquinone reductase.

A. Vinogradov, A. Ledenev, E. V. Gavrikova, 1985, Biochimica et biophysica acta.

Studies on the succinate dehydrogenating system. II. Reconstitution of succinate-ubiquinone reductase from the soluble components.

V. G. Gavrikov, A. Vinogradov, E. V. Gavrikova, 1980, Biochimica et biophysica acta.

Effect of SH‐reagents on the mitochondrial ATPase and induction of respiratory control in EDTA particle

A. Vinogradov, A. F. Fitin, Z.S. Gyurova, 1975, FEBS letters.

Unidirectional effect of lauryl sulfate on the reversible NADH:ubiquinone oxidoreductase (Complex I)

G. Cecchini, A. Vinogradov, V. G. Grivennikova, 2003, FEBS letters.

Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and the pseudo-reversible active/inactive enzyme transition.

A. Vinogradov, A D Vinogradov, 1998, Biochimica et biophysica acta.

Factors controlling the turnover number of succinate dehydrogenase: a new look at an old problem.

H. Beinert, G. A. White, A. Vinogradov, 1976, Advances in experimental medicine and biology.

Oxidation of malate by the mitochondrial succinate-ubiquinone reductase.

A. Vinogradov, A. Kotlyar, A D Vinogradov, 1988, Biochimica et biophysica acta.

Mitochondrial production of reactive oxygen species

A. Vinogradov, V. G. Grivennikova, 2013, Biochemistry (Moscow).

Mitochondrial cytochrome c oxidase and control of energy metabolism: measurements in suspensions of isolated mitochondria.

David F Wilson, D. Harrison, A. Vinogradov, 2014, Journal of applied physiology.

Allosteric nucleotide‐binding site in the mitochondrial NADH:ubiquinone oxidoreductase (respiratory complex I)

A. Vinogradov, V. G. Grivennikova, Grigory V. Gladyshev, 2011, FEBS letters.

Mitochondrial ATP synthase: fifteen years later.

A. Vinogradov, 1999, Biochemistry. Biokhimiia.

Assembly of a chimeric respiratory chain from bovine heart submitochondrial particles and cytochrome bd terminal oxidase of Escherichia coli

G. Cecchini, A. Vinogradov, V. G. Grivennikova, 2009, FEBS letters.

Partitioning of superoxide and hydrogen peroxide production by mitochondrial respiratory complex I.

A. Vinogradov, V. G. Grivennikova, Vera G Grivennikova, 2013, Biochimica et biophysica acta.

What are the sources of hydrogen peroxide production by heart mitochondria?

A. Vinogradov, V. G. Grivennikova, Alexandra V. Kareyeva, 2010, Biochimica et biophysica acta.

Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I.

G. Cecchini, J. Karliner, A. Vinogradov, 2007, Biochemistry.

Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics.

A. Vinogradov, I. Minkov, A. F. Fitin, 1982, The Biochemical journal.

Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase

A. Vinogradov, 1993, Journal of bioenergetics and biomembranes.

Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite.

A. Vinogradov, I. Minkov, A. F. Fitin, 1982, The Biochemical journal.

The Mitochondrial Complex I: Progress in Understanding of Catalytic Properties

A. Vinogradov, V. G. Grivennikova, 2001, IUBMB life.

Catalytic properties of mitochondrial NADH-ubiquinone reductase (Complex I).

N. Zakharova, A. Vinogradov, V. G. Grivennikova, 1999, Biochemistry. Biokhimiia.

Oxidative phosphorylation and respiratory control phenomenon in Paracoccus denitrificans plasma membrane

A. Vinogradov, T. V. Zharova, 2012, Biochemistry (Moscow).

Studies on the succinate dehydrogenating system. I. Kinetics of the succinate dehydrogenase interaction with a semiquindiimine radical of N,N,N',N'-tetramethyl-p-phenylenediamine.

A. Vinogradov, V. G. Grivennikova, E. V. Gavrikova, 1979, Biochimica et biophysica acta.

Reactivity of the sulfhydryl groups of soluble succinate dehydrogenase.

A. Vinogradov, E. V. Gavrikova, V. Zuevsky, 1976, European journal of biochemistry.

The catalytic activity of soluble and membrane‐bound succinate dehydrogenase

A. Vinogradov, E. V. Gavrikova, E.V. Gavrikova, 1977, FEBS letters.

The sulfhydryl groups and stability of the soluble succinate dehydrogenase

A. Vinogradov, V. Zuevsky, 1973, FEBS letters.

A new ferricyanide reactive site in soluble succinate dehydrogenase.

A. Vinogradov, E. V. Gavrikova, V. G. Goloveshkina, 1975, Biochemical and biophysical research communications.

Interaction of Mg2+ with F0.F1 mitochondrial ATPase as related to its slow active/inactive transition.

V. V. Bulygin, A. Vinogradov, 1991, The Biochemical journal.

Respiratory complex II: ROS production and the kinetics of ubiquinone reduction.

A. Vinogradov, V. G. Grivennikova, V. Kozlovsky, 2017, Biochimica et biophysica acta. Bioenergetics.

New Perspective on the Reversibility of ATP Synthesis and Hydrolysis by Fo·F1-ATP Synthase (Hydrolase)

A. Vinogradov, 2019, Biochemistry (Moscow).

Functional heterogeneity of Fo·F1H+-ATPase/synthase in coupled Paracoccus denitrificans plasma membranes.

A. Vinogradov, T. V. Zharova, 2017, Biochimica et biophysica acta. Bioenergetics.

Energy-dependent Transformation of F0·F1-ATPase in Paracoccus denitrificans Plasma Membranes*

A. Vinogradov, T. V. Zharova, 2004, Journal of Biological Chemistry.

Proton-Translocating ATP-Synthase of Paracoccus denitrificans: ATP-Hydrolytic Activity

A. Vinogradov, T. V. Zharova, 2003, Biochemistry (Moscow).

Steady-state and pre-steady-state kinetics of the mitochondrial F(1)F(o) ATPase: is ATP synthase a reversible molecular machine?

A. Vinogradov, 2000, The Journal of experimental biology.

ATP synthesis catalyzed by the mitochondrial F1‐F0 ATP synthase is not a reversal of its ATPase activity

A. Vinogradov, A. Syroeshkin, E. Vasilyeva, 1995, FEBS letters.

Three adenine nucleotide binding sites in F1‐F0 mitochondrial ATPase as revealed by presteady‐state and steady‐state kinetics of ATP hydrolysis Evidence for two inhibitory ADP‐specific noncatalytic sites

V. V. Bulygin, A. Vinogradov, 1988, FEBS letters.

[Catalytic properties of mitochondrial ATP-synthetase].

A. Vinogradov, 1984, Biokhimiia.

Kinetics of interaction of adenosine diphosphate and adenosine triphosphate with adenosine triphosphatase of bovine heart submitochondrial particles.

A. Vinogradov, I. Minkov, A. F. Fitin, 1980, The Biochemical journal.

[Isolation and properties of soluble ATPase from bovine heart mitochondria].

A. Vinogradov, V. Akimenko, I. Minkov, 1972, Biokhimiia.

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.

Interrelations of reconstitution activity, reactions with electron acceptors, and iron-sulfur centers in succinate dehydrogenase.

H. Beinert, A. Vinogradov, B. Ackrell, 1977, Archives of biochemistry and biophysics.

The initial velocities of calcium uptake by rat liver mitochondria.

A. Vinogradov, A. Scarpa, 1973, The Journal of biological chemistry.

Oxidation of NADH and ROS production by respiratory complex I.

A. Vinogradov, V. G. Grivennikova, 2016, Biochimica et biophysica acta.

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

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

FMN site‐independent energy‐linked reverse electron transfer in mitochondrial respiratory complex I

A. Vinogradov, V. G. Grivennikova, Grigory V. Gladyshev, 2018, FEBS letters.

Reversible dissociation of flavin mononucleotide from the mammalian membrane‐bound NADH:ubiquinone oxidoreductase (complex I)

G. Cecchini, A. Vinogradov, V. G. Grivennikova, 2007, FEBS letters.

Kinetics of transhydrogenase reaction catalyzed by the mitochondrial NADH‐ubiquinone oxidoreductase (Complex I) imply more than one catalytic nucleotide‐binding sites

A. Vinogradov, T. V. Zharova, N.V. Zakharova, 1999, FEBS letters.

Active/de‐active state transition of the mitochondrial complex I as revealed by specific sulfhydryl group labeling

A. Vinogradov, E. V. Gavrikova, 1999, FEBS letters.

The 29.9 kDa subunit of mitochondrial complex I is involved in the enzyme active/de-active transitions.

A. Vinogradov, M. Duarte, A. V. Ushakova, 2005, Journal of molecular biology.

Deactivation of mitochondrial NADH:ubiquinone oxidoreductase (respiratory complex I): Extrinsically affecting factors.

A. Vinogradov, V. G. Grivennikova, Grigory V. Gladyshev, 2020, Biochimica et biophysica acta. Bioenergetics.

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.

Topography and chemical reactivity of the active-inactive transition-sensitive SH-group in the mitochondrial NADH:ubiquinone oxidoreductase (Complex I).

G. Cecchini, A. Vinogradov, I. Gostimskaya, 2006, Biochimica et biophysica acta.

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 .

H+/2e- stoichiometry of the nadh:ubiquinone reductase reaction catalyzed by submitochondrial particles.

A. Vinogradov, V. G. Grivennikova, A. Galkin, 2001, Biochemistry. Biokhimiia.

Respiratory Complex I: Structure, Redox Components, and Possible Mechanisms of Energy Transduction

A. Vinogradov, 2001, Biochemistry (Moscow).

[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.

Interaction between the mitochondrial ATP synthetase and ATPase inhibitor protein

A. Vinogradov, M. V. Panchenko, 1985, FEBS letters.

The binding site for oxaloacetate on succinate dehydrogenase.

A. Vinogradov, T. King, D. Winter, 1972, Biochemical and biophysical research communications.

Identification of the high‐molecular‐mass mitochondrial oxaloacetate keto‐enol tautomerase as inactive aconitase

A. Vinogradov, A. Kotlyar, Y. Belikova, 1989, FEBS letters.

On the possible interrelations of the reactivity of soluble succinate dehydrogenase with ferricyanide, reconstitution activity, and the Hipip iron sulfur center.

A. Vinogradov, B. Ackrell, T. Singer, 1975, Biochemical and biophysical research communications.

Regulation of succinate dehydrogenase: does the membrane environment change the catalytic activity of the enzyme?

A. Vinogradov, E. V. Gavrikova, V. G. Goloveshkina, 1976, Advances in enzyme regulation.

Direct demonstration of enol‐oxaloacetate as an immediate product of malate oxidation by the mammalian succinate dehydrogenase

A. Vinogradov, M. V. Panchenko, 1991, FEBS letters.

Regulation of succinate dehydrogenase and tautomerization of oxaloacetate.

V. I. Burov, A. Vinogradov, A. Kotlyar, 1989, Advances in enzyme regulation.

The first observation of osmotically neutral sodium accumulation in the myocardial interstitium

A. Cedola, M. Fratini, A. Gianoncelli, 2021, Scientific Reports.

→H+/2e stoichiometry in NADH‐quinone reductase reactions catalyzed by bovine heart submitochondrial particles

A. Vinogradov, V. G. Grivennikova, A. Vinogradov, 1999, FEBS letters.