Online citations, reference lists, and bibliographies.
← Back to Search

Production Of Superoxide Radicals And Hydrogen Peroxide By NADH-ubiquinone Reductase And Ubiquinol-cytochrome C Reductase From Beef-heart Mitochondria.

E. Cadenas, A. Boveris, C. Ragan, A. Stoppani
Published 1977 · Chemistry, Medicine

Save to my Library
Download PDF
Analyze on Scholarcy Visualize in Litmaps
Reduce the time it takes to create your bibliography by a factor of 10 by using the world’s favourite reference manager
Time to take this seriously.
Get Citationsy
Abstract Complex I (NADH-ubiquinone reductase) and Complex III (ubiquinol-cytochrome c reductase) supplemented with NADH generated O 2 − at maximum rates of 9.8 and 6.5 nmol/min/mg of protein, respectively, while, in the presence of superoxide dismutase, the same systems generated H 2 O 2 at maximum rates of 5.1 and 4.2 nmol/min/mg of protein, respectively. H 2 O 2 was essentially produced by disproportionation of O 2 − , which constitutes the precursor of H 2 O 2 . The effectiveness of the generation of oxygen intermediates by Complex I in the absence of other specific electron acceptors was 0.95 mol of O 2 − and 0.63 mol of H 2 O 2 /mol of NADH. A reduced form of ubiquinone appeared to be responsible for the reduction of O 2 to O 2 − , since (a) ubiquinone constituted the sole common major component of Complexes I and III, (b) H 2 O 2 generation by Complex I was inhibited by rotenone, and (c) supplementation of Complex I with exogenous ubiquinones increased the rate of H 2 O 2 generation. The efficiency of added quinones as peroxide generators decreased in the order Q 1 > Q 0 > Q 2 > Q 6 = Q 10 , in agreement with the quinone capacity of acting as electron acceptor for Complex I. In the supplemented systems, the exogenous quinone was reduced by Complex I and oxidized nonenzymatically by molecular oxygen. Additional evidence for the role of ubiquinone as peroxide generator is provided by the generation of O 2 − and H 2 O 2 during autoxidation of quinols. In oxygenated buffers, ubiquinol (Q 0 H 2 ), benzoquinol, duroquinol and menadiol generated O 2 − with k 3 values of 0.1 to 1.4 m − · s −1 and H 2 O 2 with k 4 values of 0.009 to 4.3 m −1 · s −1 .
This paper references
Determination of serum proteins by means of the biuret reaction.
A. Gornall (1949)
Mechanism of the catalytic oxidation of adrenaline by ferritin.
S. Green (1956)
Identification, by electron paramagnetic resonance spectroscopy, of free radicals generated from substrates by peroxidase.
I. Yamazaki (1960)
Studies on the electron transfer system. XLI. Reduced coenzyme Q (QH2)-cytochrome c reductase.
Y. Hatefi (1962)
One-electron-transfer reactions in biochemical systems. I. Kinetic analysis of the oxidation-reduction equilibrium between quinol-quinone and ferro-ferricytochrome.
I. Yamazaki (1966)
Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles.
P. Hinkle (1967)
Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein).
J. McCord (1969)
One-electron reactions in biochemical systems as studied by pulse radiolysis. 3. Ubiquinone.
E. Land (1970)
Respiratory chain linked H2O2 production in pigeon heart mitochondria
G. Loschen (1971)
The univalent reduction of oxygen by reduced flavins and quinones.
H. Misra (1972)
The cellular production of hydrogen peroxide.
A. Boveris (1972)
The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase.
H. Misra (1972)
Experimental determination of the redox potential of the superoxide radical O 2 .
P. S. Rao (1973)
H2O2 production and cytochrome c peroxidase activity in mitochondria isolated from the trypanosomatid hemoflagellate Crithidia fasciculata.
J. Kusel (1973)
The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen.
A. Boveris (1973)
Mitochondrial H2O2 formation: Relationship with energy conservation
G. Loschen (1973)
In vitro studies on yeast cytochrome c peroxidase and its possible function in the electron transfer and energy coupling reactions.
M. Erecińska (1973)
Electron paramagnetic resonance-detectable electron acceptors in beef heart mitochondria. Reduced diphosphopyridine nucleotide ubiquinone reductase segment of the electron transfer system.
N. R. Orme-Johnson (1974)
Role of superoxide radical in mitochondrial dehydrogenase reactions.
H. Forman (1974)
Action of diethylstilbestrol on the NADH-dehydrogenase region of the respiratory chain.
M. E. de Otamendi (1974)
Superoxide radicals as precursors of mitochondrial hydrogen peroxide
G. Loschen (1974)
Properties of the S‐3 iron‐sulphur centre of succinate dehydrogenase in the intact respiratory chain of beef heart mitochondria
W. Ingledew (1975)
Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration
A. Boveris (1975)
Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues.
O. Dionisi (1975)
Superoxide production and electron transport in mitochondrial oxidation of dihydroorotic acid.
H. J. Forman (1975)
Polarographic assay and intracellular distribution of superoxide dismutase in rat liver.
D. D. Tyler (1975)
Dihydroorotate-dependent superoxide production in rat brain and liver. A function of the primary dehydrogenase.
H. Forman (1976)
Role of ubiquinone in the mitochondrial generation of hydrogen peroxide.
A. Boveris (1976)
Studies on electron paramagnetic resonance spectra manifested by a respiratory chain hydrogen carrier.
W. Ingledew (1976)
The effect of antimycin A on cytochromes b561, b566, and their relationship to ubiquinone and the iron-sulfer centers S-1 (+N-2) and S-3.
M. Erecińska (1976)

This paper is referenced by
Reactive Oxygen Species and Their Involvement in Red Blood Cell Damage in Chronic Kidney Disease
K. Gwoździński (2021)
Mitochondrial dysfunction in kidney diseases
D. Galvan (2021)
The aftermath of the interplay between the endoplasmic reticulum stress response and redox signaling
K. R. Bhattarai (2021)
The Multifaceted Roles of Zinc in Neuronal Mitochondrial Dysfunction
Hilary Y Liu (2021)
Interactions of zinc- and redox-signaling pathways
C. Hübner (2021)
Superoxide produced by mitochondrial site IQ inactivates cardiac succinate dehydrogenase and induces hepatic steatosis in Sod2 knockout mice.
H. Wong (2021)
A New Perspective on the Origin of DNA Double-Strand Breaks and Its Implications for Ageing
Bhabesh Kumar Tripathy (2021)
Scavenging reactive oxygen species mimics the anoxic response in goldfish pyramidal neurons.
Varshinie Pillai (2021)
Mitochondrial reactive oxygen species in physiology and disease.
Salvatore Antonucci (2021)
Mitochondrial calcium uniporter is essential for hearing and hair cell preservation in congenic FVB/NJ mice
M. Manikandan (2021)
Influence of Short-Term Supplementation with Anabolic Steroid Drug Oxymetholone And /Or Creatine Widely Used In Ksa on Some Fertility Biomarkers in Albino Rats
Sarah T Batais (2021)
Alterations in the Plasma and Red Blood Cell Properties in Patients with Varicose Vein: A Pilot Study
L. Gwozdzinski (2021)
Coenzyme Q10 Analogues: Benefits and Challenges for Therapeutics
J. M. Suárez-Rivero (2021)
Mitochondrial Glutathione: Recent Insights and Role in Disease
M. Marí (2020)
The Bioactivity of Neuronal-Derived Nitric Oxide in Aging and Neurodegeneration: Switching Signaling to Degeneration.
A. Ledo (2020)
A functional analysis of mitochondrial respiratory chain cytochrome bc 1 complex in Gaeumannomyces tritici by RNA silencing as a possible target of carabrone
M. Wang (2020)
Temporal evolution of cardiac mitochondrial dysfunction in a type 1 Diabetes model. Mitochondrial complex I impairment, and H2O2 and NO productions as early subcellular events.
Ivana A. Rukavina-Mikusic (2020)
Attenuation of arsenic induced high fat diet exacerbated oxidative stress mediated hepatic and cardiac injuries in male Wistar rats by piperine involved antioxidative mechanisms.
T. Dey (2020)
Mitochondrial unfolded protein-related responses across kingdoms: similar problems, different regulators.
Huy Cuong Tran (2020)
Mitochondrial ROS production during ischemia-reperfusion injury
H. Prag (2020)
Human mitochondrial DNA repair
E. Sia (2020)
Manipulating Cellular Energetics to Slow Aging of Tissues and Organs
S. Sokolov (2020)
Glutathione in Brain: Overview of Its Conformations, Functions, Biochemical Characteristics, Quantitation and Potential Therapeutic Role in Brain Disorders
Divya Dwivedi (2020)
Mechanisms of Mitochondrial ROS Production in Assisted Reproduction: The Known, the Unknown, and the Intriguing
J. Cobley (2020)
New properties of vitamin B6 or pyridoxine in experimental oxidative stress in the brain
K. Danielyan (2020)
SIRT1 Activation by Polydatin Alleviates Oxidative Damage and Elevates Mitochondrial Biogenesis in Experimental Diabetic Neuropathy
Preethi Bheereddy (2020)
Mitochondrial unfolded protein-related responses across kingdoms: similar problems, different regulators.
Huy Cuong Tran (2020)
From Past to Present: The Link Between Reactive Oxygen Species in Sperm and Male Infertility
A. Villaverde (2019)
Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling
John J. Skoko (2019)
NADPH oxidases and oxidase crosstalk in cardiovascular diseases: novel therapeutic targets
Y. Zhang (2019)
Age-dependent hippocampal network dysfuntion in a mouse model of alpha-synucleinopathy
Clare Tweedy (2019)
Flow-cytometry-based physiological characterisation and transcriptome analyses reveal a mechanism for reduced cell viability in yeast engineered for increased lipid content
Huadong Peng (2019)
See more
Semantic Scholar Logo Some data provided by SemanticScholar