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Respiratory Chain Linked H2O2 Production In Pigeon Heart Mitochondria

G. Loschen, L. Flohé
Published 1971 · Chemistry, Medicine

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It has been known for many years that the succinate dehydrogenase of the intestinal nematode Ascaris lumbricoides reacts with molecular oxygen without participation of the cytochrome system under formation of HaOa [l-3] . Besides, P.K. Jensen reported that at least part of the antimycin insensitive respiration of beef heart ETPs might be due to HaOa formation [4]. It was assumed that NADH was the autoxidable component of the resplratory chain responsible for the H1Oa generation. P. Hinkle et al. [5] presented evidence for an ATP dependent HaOa formation on the substrate side of cytochrome b in submitochondrial particles of beef heart. But all these results require experimental corroboration because no method had been available for determining low concentrations of HzOZ in biological material directly. Recently, Chance and Oshino [6] approached this problem in the following way: preparations of rat liver mitochondria were observed with a dual wavelength spectrophotometer. Formation of compound I of peroxisomal catalase present in these preparations was considered indicative of HzOz . In the present study HZOz was determined by the horse radish peroxidase dependent reaction of HzOZ with the fluorescent dye scopoletine [7]. A decrease ‘of fluorescence intensity demonstrates directly the
This paper references
10.1016/0926-6593(66)90057-9
Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation.
P. K. Jensen (1966)
10.1016/0005-2728(70)90131-3
The oxidase systems of Ascaris-muscle mitochondria.
K. S. Cheah (1970)
Flavin and pyridine nucleotide oxidation-reduction changes in perfused rat liver. I. Anoxia and subcellular localization of fluorescent flavoproteins.
R. Scholz (1969)
10.1038/175859A0
A Sensitive Method for the Estimation of Hydrogen Peroxide in Biological Materials
W. Andreae (1955)
10.1016/s0021-9258(18)57021-6
Determination of serum proteins by means of the biuret reaction.
A. Gornall (1949)
10.1016/s0021-9258(18)64408-4
Succinic and reduced diphosphopyridine nucleotide oxidase systems of Ascaris muscle.
E. Kmetec (1961)
10.1083/JCB.37.2.482
THE LARGE-SCALE SEPARATION OF PEROXISOMES, MITOCHONDRIA, AND LYSOSOMES FROM THE LIVERS OF RATS INJECTED WITH TRITON WR-1339
F. Leighton (1968)
10.1038/190257A0
Determination of Very Small Amounts of Hydrogen Peroxide
H. Perschke (1961)
10.1042/BJ1220225
Kinetics and mechanisms of catalase in peroxisomes of the mitochondrial fraction.
B. Chance (1971)
10.1016/s0021-9258(18)96643-3
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)
10.1016/s0021-9258(19)52396-1
Cytochrome c, cytochrome oxidase, and succinoxidase activities of helminths.
E. Bueding (1952)



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10.3390/nu11122900
Vitamin E Supplementation and Mitochondria in Experimental and Functional Hyperthyroidism: A Mini-Review
G. Napolitano (2019)
10.1111/cmi.12250
The C2 fragment from Neisseria meningitidis antigen NHBA increases endothelial permeability by destabilizing adherens junctions
A. Casellato (2014)
C 2 Fragment from Neisseria meningitidis Antigen NHBA Disassembles Adherence Junctions of Brain Microvascular Endothelial Cells
(2013)
10.1111/J.1095-8649.1996.TB00095.X
Antioxidant enzyme activities in embryologic and early larval stages of turbot
L. Peters (1996)
10.1016/0005-2728(74)90145-5
The respiratory system of the marine bacterium Beneckea natriegens. II. Terminal branching of respiration to oxygen and resistance to inhibition by cyanide.
J. Weston (1974)
10.1007/BF01002750
An enzyme histochemical study of isoproterenol-induced myocardial necroses in rats
A. E. Meijer (2005)
10.1074/jbc.M110.101196
Respiration-dependent H2O2 Removal in Brain Mitochondria via the Thioredoxin/Peroxiredoxin System*
Derek A. Drechsel (2010)
10.1007/BF00503828
Potentiation of the insulin-releasing capacity of tolbutamide by thiols: Studies on the isolated perfused pancreas
H. Ammon (2004)
10.1152/ajpendo.00374.2009
Increased basal level of Akt-dependent insulin signaling may be responsible for the development of insulin resistance.
H. Liu (2009)
10.1007/978-94-009-2697-4_19
The Cardiac Defense System Associated with Glutathione
Toshihisa Ishikawa (1988)
10.1016/B978-0-12-566505-6.50010-7
CHAPTER 3 – Superoxide Radical and Hydrogen Peroxide in Mitochondria
H. Forman (1982)
10.1523/JNEUROSCI.1842-04.2004
Generation of Reactive Oxygen Species in the Reaction Catalyzed by α-Ketoglutarate Dehydrogenase
L. Tretter (2004)
10.1016/b978-0-12-801238-3.01895-x
1.14 – Free Radicals and Reactive Oxygen Species☆
A. Siraki (2018)
10.1111/j.1742-4658.2010.07693.x
Hydrogen peroxide efflux from muscle mitochondria underestimates matrix superoxide production – a correction using glutathione depletion
J. Treberg (2010)
10.1016/J.BBRC.2005.06.147
Synoviocytes, not chondrocytes, release free radicals after cycles of anoxia/re-oxygenation.
N. Schneider (2005)
10.1016/S0300-483X(98)00093-6
Cellular and subcellular heterogeneity of glutathione metabolism and transport in rat kidney cells.
L. Lash (1998)
10.3109/10408449309104073
Free radicals as mediators of tissue injury and disease.
J. Kehrer (1993)
10.1111/J.1365-201X.2004.01370.X
Ageing, oxidative stress, and mitochondrial uncoupling.
M. Harper (2004)
10.5451/UNIBAS-006450386
Studies on the role of two proteins in breast cancer - histone deacetylase 11 in estrogen receptor positive breast cancer and the redox protein memo in metastasis and tumorigenesis
Anna Frei (2015)
10.1016/j.bcp.2008.08.021
The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation.
Andrew G. Cox (2008)
10.1210/en.2011-2119
Prolonged exposure to insulin induces mitochondrion-derived oxidative stress through increasing mitochondrial cholesterol content in hepatocytes.
Shuang Mei (2012)
10.1534/genetics.111.133660
No Evidence of Elevated Germline Mutation Accumulation Under Oxidative Stress in Caenorhabditis elegans
J. Joyner-Matos (2011)
10.1023/A:1005427919188
Mitochondrial Oxygen Radical Generation and Leak: Sites of Production in States 4 and 3, Organ Specificity, and Relation to Aging and Longevity
G. Barja (1999)
10.1007/978-3-319-45865-6_3
Mitochondria Are the Main Cellular Source of O 2 − , H 2 O 2 and Oxidative Stress
A. Boveris (2016)
10.1016/j.bbagen.2015.12.007
A hydrogen peroxide safety valve: The reversible phosphorylation of catalase from the freeze-tolerant North American wood frog, Rana sylvatica.
N. J. Dawson (2016)
10.1016/S0076-6879(10)73001-9
Changing paradigms in thiology from antioxidant defense toward redox regulation.
L. Flohé (2010)
10.2741/S495
Oxidative stress: Major executioner in disease pathology, role in sperm DNA damage and preventive strategies.
S. Bisht (2017)
10.1016/0022-4804(86)90017-X
Protection against oxygen-induced reperfusion injury of the isolated canine heart by superoxide dismutase and catalase.
H. Otani (1986)
10.1016/0167-4838(84)90028-1
Hydroxyl free radical reactions with amino acids and proteins studied by electron spin resonance spectroscopy and spin-trapping.
I. Nagy (1984)
10.1016/0006-291X(90)92004-J
Glutathione depletion and formation of glutathione-protein mixed disulfide following exposure of brain mitochondria to oxidative stress.
V. Ravindranath (1990)
10.1016/0014-5793(78)80537-7
Evidence for the existence of catalase in the matrix space of rat‐heart mitochondria
H. Nohl (1978)
10.1007/978-3-7091-1001-0_12
Oxidative stress in neurodegeneration: targeting mitochondria as a therapeutic aid
E. Gaggelli (2012)
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