Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)

High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria

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Topology of superoxide production from different sites in the mitochondrial electron transport chain

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Generation of reactive oxygen species by the mitochondrial electron transport chain

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The sites and topology of mitochondrial superoxide production

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The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria

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Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state

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Regulation of brain mitochondrial H 2 O 2 production by membrane potential and NAD(P)H redox state

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Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial nadh:Ubiquinone oxidoreductase (complex i)

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Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane

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Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age

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Generation of superoxide by the mitochondrial Complex I

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The production of reactive oxygen species by complex I

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Superoxide Is Produced by the Reduced Flavin in Mitochondrial Complex I

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Superoxide and hydrogen peroxide production by Drosophila mitochondria

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The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron–sulfur cluster N2

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Characteristics of mitochondrial proton leak and control of oxidative phosphorylation in the major oxygen-consuming tissues of the rat

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Differential effects of mitochondrial Complex I inhibitors on production of reactive oxygen species

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On the Redox Potentials of Ubiquinone and Cytochrome b in the Respiratory Chain

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Localization of the Site of Oxygen Radical Generation inside the Complex I of Heart and Nonsynaptic Brain Mammalian Mitochondria

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Production of Reactive Oxygen Species by Complex I (NADH:Ubiquinone Oxidoreductase) from Escherichia coli and Comparison to the Enzyme from Mitochondria

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Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase.

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A Possible Site of Superoxide Generation in the Complex I Segment of Rat Heart Mitochondria

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

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

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Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio

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Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production – a correction using glutathione depletion

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Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoraductase by rotenone, piericidin A, and MPP+

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Inhibition of the alpha‐ketoglutarate dehydrogenase‐mediated reactive oxygen species generation by lipoic acid

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New insights into the superoxide generation sites in bovine heart NADH-ubiquinone oxidoreductase (Complex I): The significance of protein-associated ubiquinone and the dynamic shifting of generation sites between semiflavin and semiquinone radicals

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A Model of the Proton Translocation Mechanism of Complex I

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Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state

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Mechanisms of Mitochondrial Free Radical Production and their Relationship to the Aging Process

Quinlan, C. L., Treberg, J. R., & Brand, M. D. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-378638-8.00003-8 · Cited by 12 · see citing works

Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling

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Mitochondrial Complex II Can Generate Reactive Oxygen Species at High Rates in Both the Forward and Reverse Reactions

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Superoxide generation by complex III: From mechanistic rationales to functional consequences

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Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise

Goncalves, R. L. S., Quinlan, C. L., Perevoshchikova, I. V., Hey-Mogensen, M., & Brand, M. D. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.619072 · Cited by 329 · see citing works

Functional role of mitochondrial respiratory supercomplexes

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The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I

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Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning

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Sources and implications of NADH/NAD+ redox imbalance in diabetes and its complications

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Inhibitors of succinate: quinone reductase/complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death

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Inhibitors of ros production by the ubiquinone-binding site of mitochondrial complex i identified by chemical screening

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Antioxidant Mechanism of Mitochondria-Targeted Plastoquinone SkQ1 Is Suppressed in Aglycemic HepG2 Cells Dependent on Oxidative Phosphorylation

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New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles

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Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)

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