Andrei D. Vinogradov

University of Tyumen

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Vera G. Grivennikova

Lomonosov Moscow State University

Tatyana V. Zharova

Lomonosov Moscow State University

Eleonora V. Gavrikova

Lomonosov Moscow State University

Alexander Kotlyar

Tel Aviv University

Vladimir D. Sled

University of Pennsylvania

Gary Cecchini

University of California, San Francisco

I. Minkov

Sofia University "St. Kliment Ohridski"

Elena Vasilyeva

Siberian State Medical University

A.F. Fitin

Lomonosov Moscow State University

D. Sh. Burbaev

Russian Academy of Sciences

Cooperative Institutions

Lomonosov Moscow State University

Russian Academy of Sciences

Moscow State University

Centre National de la Recherche Scientifique

University of California, San Francisco

University of Pennsylvania

National Institutes of Health

Ministry of Health of the Russian Federation

Institute of Bioorganic Chemistry

Karolinska Institutet

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Steady-State and Pre-Steady-State Kinetics of the Mitochondrial F1Fo ATPase: Is Atp Synthase a Reversible Molecular Machine?

Journal of Experimental Biology (2000)

Andrei D. Vinogradov

ABSTRACT H+-ATP synthase (F1Fo ATPase) catalyzes the synthesis and/or hydrolysis of ATP, and the reactions are strongly affected by all the substrates (products) in a way clearly distinct from that expected of a simple reversibly operating enzyme. Recent studies have revealed the structure of F1, which is ideally suited for the alternating binding change mechanism, with a rotating γ-subunit as the energy-driven coupling device. According to this mechanism ATP, ADP, inorganic phosphate (Pi) and Mg2+ participate in the forward and reverse overall reactions exclusively as the substrates and products. However, both F1 and F1Fo demonstrate non-trivial steady-state and pre-steady-state kinetics as a function of variable substrate (product) concentrations. Several effectors cause unidirectional inhibition or activation of the enzyme. When considered separately, the unidirectional effects of ADP, Pi, Mg2+ and energy supply on ATP synthesis or hydrolysis may possibly be explained by very complex kinetic schemes; taken together, the results suggest that different conformational states of the enzyme operate in the ATP hydrolase and ATP synthase reactions. A possible mechanism for an energy-dependent switch between the two states of F1Fo ATPase is proposed.

Chemiosmosis

F-ATPase

Adenosine triphosphate

V-ATPase

10.1242/jeb.203.1.41

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Citations (89)

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

Biochimica et Biophysica Acta (BBA) - Bioenergetics (1997)

Vera G. Grivennikova Elena Maklashina Eleonora V. Gavrikova Andrei D. Vinogradov

Rotenone

Ubiquinol

10.1016/s0005-2728(96)00163-6

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Citations (66)

Respiratory complex II catalyzed ROS product ion

Vera G. Grivennikova Andrei D. Vinogradov

Source

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

FEBS Letters (1989)

D. Sh. Burbaev I.A. Moroz Alexander Kotlyar Vladimir D. Sled Andrei D. Vinogradov

Coupled bovine heart submitochondrial particles exhibit a rotenone‐sensitive g = 2.00 low‐temperature EPR signal attributable to ubisemiquinone which is observed during steady‐state electron transfer from NADH to oxygen or from succinate to NAD + in Δµ̃H + ‐dependent reverse electron transfer. Quantitation of the signal under optimal conditions gives a value for maximal semiquinone of approx. 0.5 spins per spin of the fully reduced NADH dehydrogenase iron‐sulfur center N‐2. The intensity of the signal is drastically reduced when electron transfer from NADH to oxygen is blocked by cyanide or in the case of the reverse electron transfer from succinate to NAD + being prevented by anaerobiosis. Only those particles which contain ‘turnover‐preconditioned” NADH‐ubiquinone reductase demonstrate the ubisemiquinone signal together with N‐1, N‐2, N‐3 and N‐4 iron‐sulfur centers. The spin relaxation characteristics of the rotenone‐sensitive ubisemiquinone signal point to its interaction with one of the rapidly relaxing (4Fe‐4S) centers, most probably N‐2.

Submitochondrial particle

Semiquinone

NADH dehydrogenase

10.1016/0014-5793(89)81007-5

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Citations (74)

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

Biochimica et Biophysica Acta (BBA) - Bioenergetics (1980)

Andrei D. Vinogradov Victor G. Gavrikov Eleonora V. Gavrikova

Submitochondrial particle

Thenoyltrifluoroacetone

Turnover number

Fraction (chemistry)

Electron acceptor

10.1016/0005-2728(80)90110-3

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Redox-Dependent Change of Nucleotide Affinity to the Active Site of the Mammalian Complex I

Biochemistry (2007)

Vera G. Grivennikova Alexander Kotlyar Joel S. Karliner Gary Cecchini Andrei D. Vinogradov

A very potent and specific inhibitor of mitochondrial NADH:ubiquinone oxidoreductase (complex I), a derivative of NADH (NADH-OH) has recently been discovered (Kotlyar, A. B., Karliner, J. S., and Cecchini, G. (2005) FEBS Lett. 579, 4861−4866). Here we present a quantitative analysis of the interaction of NADH-OH and other nucleotides with oxidized and reduced complex I in tightly coupled submitochondrial particles. Both the rate of the NADH-OH binding and its affinity to complex I are strongly decreased in the presence of succinate. The effect of succinate is completely reversed by rotenone, antimycin A, and uncoupler. The relative affinity of ADP-ribose, a competitive inhibitor of NADH oxidation, is also shown to be significantly affected by enzyme reduction (KD of 30 and 500 μM for oxidized and the succinate-reduced enzyme, respectively). Binding of NADH-OH is shown to abolish the succinate-supported superoxide generation by complex I. Gradual inhibition of the rotenone-sensitive uncoupled NADH oxidase and the reverse electron transfer activities by NADH-OH yield the same final titration point (∼0.1 nmol/mg of protein). The titration of NADH oxidase appears as a straight line, whereas the titration of the reverse reaction appears as a convex curve. Possible models to explain the different titration patterns for the forward and reverse reactions are briefly discussed.

Submitochondrial particle

Antimycin A

Rotenone

NADH dehydrogenase

10.1021/bi7009822

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Citations (37)

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

Biochimica et Biophysica Acta (BBA) - Bioenergetics (1985)

P.R. Tushurashvili Eleonora V. Gavrikova Alexander N. Ledenev Andrei D. Vinogradov

Ferricyanide

Submitochondrial particle