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

Grivennikova, Vera G / Gladyshev, Grigory V / Vinogradov, Andrei D

Biochimica et biophysica acta. Bioenergetics

2020 Volume 1861, Issue 8, Page(s) 148207

Abstract: Mitochondrial NADH:ubiquinone oxidoreductase (proton translocating respiratory complex I) serves several essential functions in cell metabolism: it maintains the intramitochondrial NADH/ ... ...

Abstract	Mitochondrial NADH:ubiquinone oxidoreductase (proton translocating respiratory complex I) serves several essential functions in cell metabolism: it maintains the intramitochondrial NADH/NAD
MeSH term(s)	Animals ; Cattle ; Cell Membrane/metabolism ; Electron Transport Complex I/chemistry ; Electron Transport Complex I/metabolism ; Enzyme Activation ; Kinetics ; Mitochondria/enzymology ; Protein Unfolding ; Protons
Chemical Substances	Protons ; Electron Transport Complex I (EC 7.1.1.2)
Language	English
Publishing date	2020-04-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2020.148207
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Article: Functional heterogeneity of F

Zharova, Tatyana V / Vinogradov, Andrei D

Biochimica et biophysica acta. Bioenergetics

2017 Volume 1858, Issue 11, Page(s) 939–944

Abstract: ... ...

Abstract	F
MeSH term(s)	Adenosine Diphosphate/chemistry ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/chemistry ; Adenosine Triphosphate/metabolism ; Cell Membrane/chemistry ; Hydrogen-Ion Concentration ; Ion Transport ; Isoenzymes/chemistry ; Isoenzymes/metabolism ; Kinetics ; Paracoccus denitrificans/chemistry ; Paracoccus denitrificans/enzymology ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; Proton-Translocating ATPases/chemistry ; Proton-Translocating ATPases/metabolism ; Venturicidins/chemistry
Chemical Substances	Isoenzymes ; Protein Subunits ; Venturicidins ; venturicidin (11021-88-8) ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Proton-Translocating ATPases (EC 3.6.3.14)
Language	English
Publishing date	2017-08-10
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0005-2728 ; 0006-3002 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0005-2728 ; 0006-3002 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2017.08.006
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Article: Oxidation of NADH and ROS production by respiratory complex I.

Vinogradov, Andrei D / Grivennikova, Vera G

Biochimica et biophysica acta

2016 Volume 1857, Issue 7, Page(s) 863–871

Abstract: Kinetic characteristics of the proton-pumping NADH:quinone reductases (respiratory complexes I) are reviewed. Unsolved problems of the redox-linked proton translocation activities are outlined. The parameters of complex I-mediated superoxide/hydrogen ... ...

Abstract	Kinetic characteristics of the proton-pumping NADH:quinone reductases (respiratory complexes I) are reviewed. Unsolved problems of the redox-linked proton translocation activities are outlined. The parameters of complex I-mediated superoxide/hydrogen peroxide generation are summarized, and the physiological significance of mitochondrial ROS production is discussed. This article is part of a Special Issue entitled Respiratory complex I, edited by Volker Zickermann and Ulrich Brandt.
MeSH term(s)	Electron Transport ; Electron Transport Complex I/chemistry ; Electron Transport Complex I/ultrastructure ; Enzyme Activation ; Models, Chemical ; Molecular Dynamics Simulation ; NAD/chemistry ; NAD/ultrastructure ; Oxidation-Reduction ; Protein Conformation ; Proton Pumps/chemistry ; Proton Pumps/ultrastructure ; Reactive Oxygen Species/chemical synthesis
Chemical Substances	Proton Pumps ; Reactive Oxygen Species ; NAD (0U46U6E8UK) ; Electron Transport Complex I (EC 1.6.5.3)
Language	English
Publishing date	2016-07
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2015.11.004
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Article ; Online: FMN site-independent energy-linked reverse electron transfer in mitochondrial respiratory complex I.

Gladyshev, Grigory V / Grivennikova, Vera G / Vinogradov, Andrei D

FEBS letters

2018 Volume 592, Issue 13, Page(s) 2213–2219

Abstract: A simple assay procedure for measuring ATP-dependent reverse electron transfer from ubiquinol to hexaammineruthenium (III) (HAR) catalyzed by mitochondrial respiratory complex I is introduced. The specific activity of the enzyme in this reaction and its ... ...

Abstract	A simple assay procedure for measuring ATP-dependent reverse electron transfer from ubiquinol to hexaammineruthenium (III) (HAR) catalyzed by mitochondrial respiratory complex I is introduced. The specific activity of the enzyme in this reaction and its sensitivity to the standard inhibitors and uncoupling are the same as with other well-known electron acceptors, NAD
MeSH term(s)	Animals ; Binding Sites ; Cattle ; Electron Transport/physiology ; Electron Transport Complex I/chemistry ; Electron Transport Complex I/metabolism ; Electrons ; Energy Transfer/physiology ; Flavin Mononucleotide/chemistry ; Flavin Mononucleotide/metabolism ; In Vitro Techniques ; Mitochondria/metabolism ; Mitochondria, Heart/drug effects ; Mitochondria, Heart/metabolism ; Oxidation-Reduction ; Ruthenium Compounds/chemistry ; Ruthenium Compounds/pharmacology
Chemical Substances	Ruthenium Compounds ; hexammineruthenium (19052-44-9) ; Flavin Mononucleotide (7N464URE7E) ; Electron Transport Complex I (EC 1.6.5.3)
Language	English
Publishing date	2018-06-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13117
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Article ; Online: Oxygen-dependence of mitochondrial ROS production as detected by Amplex Red assay.

Grivennikova, Vera G / Kareyeva, Alexandra V / Vinogradov, Andrei D

Redox biology

2018 Volume 17, Page(s) 192–199

Abstract: The initial rates of superoxide plus hydrogen peroxide (ROS) generation by intact or permeabilized rat heart mitochondria and coupled inside-out bovine heart submitochondrial particles (SMP) oxidizing NAD-dependent substrates, NADH, and succinate were ... ...

Abstract	The initial rates of superoxide plus hydrogen peroxide (ROS) generation by intact or permeabilized rat heart mitochondria and coupled inside-out bovine heart submitochondrial particles (SMP) oxidizing NAD-dependent substrates, NADH, and succinate were measured by detecting resorufin formation in the Amplex Red assay at various oxygen concentrations. Linear dependences of the initial rates on oxygen concentration within the range of ~125-750 μM were found for all significant mitochondrial generators, i.e. the respiratory complexes and ammonium-stimulated dihydrolipoamide dehydrogenase. At lower oxygen concentrations upon its decrease from air saturation level to zero, the time-course of resorufin formation by SMP catalyzing coupled oxidation of succinate (the total ROS production by respiratory complexes II and III and by the reverse electron transfer (RET)-mediated by complex I) also corresponds to the linear dependence on oxygen with the same first-order rate constant determined in the initial rate studies. Prolonged incubation of SMP generating succinate-supported complex I-mediated ROS affected neither their NADH oxidase nor ROS generating activity. In contrast to SMP significant deviation from the first-order oxygen dependence in the time-course kinetics during coupled oxidation of succinate by intact mitochondria was evident. Complex I catalyzes the NADH:resorufin oxidoreductase reaction resulting in formation of colorless reduced resorufin. Hydrogen peroxide oxidizes reduced resorufin in the presence of peroxidase, thus showing its dihydroresorufin peroxidase activity. Combined NADH:resorufin reductase and dihydroresorufin peroxidase activities result in underestimation of the amount of hydrogen peroxide generated by mitochondria. We conclude that only initial rates of the mitochondrial ROS production, not the amount of resorufin accumulated, should be taken as the reliable measure of the mitochondrial ROS-generating activity, because of the cycling of the oxidized and reduced resorufin during Amplex Red assays fed by NADH and other possible reductant(s) present in mitochondria.
MeSH term(s)	Animals ; Electron Transport/genetics ; Electron Transport Complex I/genetics ; Electron Transport Complex I/metabolism ; Electron Transport Complex II/genetics ; Electron Transport Complex II/metabolism ; Hydrogen Peroxide/chemistry ; Mitochondria, Heart/metabolism ; NAD/metabolism ; Oxazines/chemistry ; Oxazines/isolation & purification ; Oxazines/metabolism ; Oxidation-Reduction ; Oxygen/metabolism ; Rats ; Reactive Oxygen Species/metabolism ; Succinic Acid/metabolism ; Superoxides/chemistry
Chemical Substances	Oxazines ; Reactive Oxygen Species ; respiratory complex II ; NAD (0U46U6E8UK) ; Superoxides (11062-77-4) ; Amplex Red (119171-73-2) ; resorufin (635-78-9) ; Succinic Acid (AB6MNQ6J6L) ; Hydrogen Peroxide (BBX060AN9V) ; Electron Transport Complex II (EC 1.3.5.1) ; Electron Transport Complex I (EC 7.1.1.2) ; Oxygen (S88TT14065)
Language	English
Publishing date	2018-04-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701011-9
ISSN	2213-2317 ; 2213-2317
ISSN (online)	2213-2317
ISSN	2213-2317
DOI	10.1016/j.redox.2018.04.014
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Article ; Online: Quantifying the Efficacy of Magnetic Nanoparticles for MRI and Hyperthermia Applications via Machine Learning Methods.

Kim, Pavel / Serov, Nikita / Falchevskaya, Aleksandra / Shabalkin, Ilia / Dmitrenko, Andrei / Kladko, Daniil / Vinogradov, Vladimir

Small (Weinheim an der Bergstrasse, Germany)

2023 Volume 19, Issue 48, Page(s) e2303522

Abstract: Magnetic nanoparticles are a prospective class of materials for use in biomedicine as agents for magnetic resonance imagining (MRI) and hyperthermia treatment. However, synthesis of nanoparticles with high efficacy is resource-intensive experimental work. ...

Abstract	Magnetic nanoparticles are a prospective class of materials for use in biomedicine as agents for magnetic resonance imagining (MRI) and hyperthermia treatment. However, synthesis of nanoparticles with high efficacy is resource-intensive experimental work. In turn, the use of machine learning (ML) methods is becoming useful in materials design and serves as a great approach to designing nanomagnets for biomedicine. In this work, for the first time, an ML-based approach is developed for the prediction of main parameters of material efficacy, i.e., specific absorption rate (SAR) for hyperthermia and r
MeSH term(s)	Magnetite Nanoparticles ; Prospective Studies ; Magnetic Resonance Imaging/methods ; Hyperthermia, Induced/methods ; Magnetic Resonance Spectroscopy
Chemical Substances	Magnetite Nanoparticles
Language	English
Publishing date	2023-08-10
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2168935-0
ISSN	1613-6829 ; 1613-6810
ISSN (online)	1613-6829
ISSN	1613-6810
DOI	10.1002/smll.202303522
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Article ; Online: Coordination Polymers of Polyphenyl-Substituted Potassium Cyclopentadienides.

Komarov, Pavel D / Birin, Kirill P / Vinogradov, Alexander A / Varaksina, Evgenia A / Puntus, Lada N / Lyssenko, Konstantin A / Churakov, Andrei V / Nifant'ev, Ilya E / Minyaev, Mikhail E / Roitershtein, Dmitrii M

Molecules (Basel, Switzerland)

2022 Volume 27, Issue 22

Abstract: A series of potassium salts of di- and tri-arylsubstituted cyclopentadienes has been obtained by the metalation of the corresponding cyclopentadienes with benzylpotassium in THF media. Crystals of all compounds, afforded by recrystallization from THF/ ... ...

Abstract	A series of potassium salts of di- and tri-arylsubstituted cyclopentadienes has been obtained by the metalation of the corresponding cyclopentadienes with benzylpotassium in THF media. Crystals of all compounds, afforded by recrystallization from THF/hexane, diglyme-THF/hexane and toluene/hexane mixtures, have been studied by X-ray diffraction. All studied potassium cyclopentadienides exhibit the luminescence at room temperature and overall quantum yield of photoluminescence for potassium salt of diarylsubstituted cyclopentadiene is 18%.
Language	English
Publishing date	2022-11-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules27227725
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Article: NADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I).

Vinogradov, Andrei D

Biochimica et biophysica acta

2008 Volume 1777, Issue 7-8, Page(s) 729–734

Abstract: The quantitative data on the binding affinity of NADH, NAD(+), and their analogues for complex I as emerged from the steady-state kinetics data and from more direct studies under equilibrium conditions are summarized and discussed. The redox-dependency ... ...

Abstract	The quantitative data on the binding affinity of NADH, NAD(+), and their analogues for complex I as emerged from the steady-state kinetics data and from more direct studies under equilibrium conditions are summarized and discussed. The redox-dependency of the nucleotide binding and the reductant-induced change of FMN affinity to its tight non-covalent binding site indicate that binding (dissociation) of the substrate (product) may energetically contribute to the proton-translocating activity of complex I.
MeSH term(s)	Animals ; Bacterial Proteins/metabolism ; Electron Transport Complex I/metabolism ; Energy Metabolism ; Kinetics ; Mitochondria/enzymology ; NAD/metabolism ; Oxidation-Reduction ; Oxygen Consumption ; Submitochondrial Particles/enzymology
Chemical Substances	Bacterial Proteins ; NAD (0U46U6E8UK) ; Electron Transport Complex I (EC 7.1.1.2)
Language	English
Publishing date	2008-04-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2008.04.014
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Article: ATPase/synthase activity of Paracoccus denitrificans Fo·F1 as related to the respiratory control phenomenon.

Zharova, Tatyana V / Vinogradov, Andrei D

Biochimica et biophysica acta

2014 Volume 1837, Issue 8, Page(s) 1322–1329

Abstract: The time course of ATP synthesis, oxygen consumption, and change in the membrane potential in Paracoccus denitrificans inside-out plasma membrane vesicles was traced. ATP synthesis initiated by the addition of a limited amount of either ADP or inorganic ... ...

Abstract	The time course of ATP synthesis, oxygen consumption, and change in the membrane potential in Paracoccus denitrificans inside-out plasma membrane vesicles was traced. ATP synthesis initiated by the addition of a limited amount of either ADP or inorganic phosphate proceeded up to very low residual concentrations of the limiting substrate. Accumulated ATP did not decrease the rate of its synthesis initiated by the addition of ADP. The amount of residual ADP determined at State 4 respiration was independent of ten-fold variation of Pi or the presence of ATP. The pH-dependence of Km for Pi could not be fitted to a simple phosphoric acid dissociation curve. Partial inhibition of respiration resulted in a decrease in the rate of ATP synthesis without affecting the ATP/ADP reached at State 4. At pH8.0, hydrolysis of ATP accumulated at State 4 was induced by a low concentration of an uncoupler, whereas complete uncoupling results in rapid inactivation of ATPase. At pH7.0, no reversal of the ATP synthase reaction by the uncoupler was seen. The data show that ATP/ADP×Pi ratio maintained at State 4 is not in equilibrium with respiratory-generated driving force. Possible mechanisms of kinetic control and unidirectional operation of the Fo·F1-ATP synthase are discussed.
MeSH term(s)	Adenosine Diphosphate/biosynthesis ; Adenosine Diphosphate/chemistry ; Adenosine Triphosphate/biosynthesis ; Adenosine Triphosphate/chemistry ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Ion Transport ; Kinetics ; Oxidative Phosphorylation ; Oxygen Consumption ; Paracoccus denitrificans/enzymology ; Phosphates/chemistry ; Phosphates/metabolism ; Proton-Translocating ATPases/chemistry ; Proton-Translocating ATPases/metabolism
Chemical Substances	Phosphates ; Adenosine Diphosphate (61D2G4IYVH) ; Adenosine Triphosphate (8L70Q75FXE) ; Proton-Translocating ATPases (EC 3.6.3.14)
Language	English
Publishing date	2014-08
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbabio.2014.04.002
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Article: Oxidation of NADH and ROS production by respiratory complex I

Vinogradov, Andrei D / Vera G. Grivennikova

Biochimica et biophysica acta. 2016 July, v. 1857, no. 7

2016

Abstract	Kinetic characteristics of the proton-pumping NADH:quinone reductases (respiratory complexes I) are reviewed. Unsolved problems of the redox-linked proton translocation activities are outlined. The parameters of complex I-mediated superoxide/hydrogen peroxide generation are summarized, and the physiological significance of mitochondrial ROS production is discussed. This article is part of a Special Issue entitled Respiratory complex I, edited by Volker Zickermann and Ulrich Brandt.
Keywords	NAD (coenzyme) ; hydrogen peroxide ; mitochondria ; oxidation
Language	English
Dates of publication	2016-07
Size	p. 863-871.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	282711-6
ISSN	0005-2728 ; 0304-4173
ISSN	0005-2728 ; 0304-4173
DOI	10.1016/j.bbabio.2015.11.004
Database	NAL-Catalogue (AGRICOLA)

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