Detection of catalase in rat heart mitochondria.
Open accessAbstract
The presence of heme-containing catalase in rat heart mitochondria (20 +/- 5 units/mg) was demonstrated by biochemical and immunocytochemical analysis. Intact rat heart mitochondria efficiently consumed exogenously added H2O2. The rate of H2O2 consumption was not influenced by succinate, glutamate/malate, or N-ethylmaleimide but was significantly inhibited by cyanide. Hydrogen peroxide decomposition by mitochondria yielded molecular oxygen in a 2:1 stoichiometry, consistent with a catalytic mechanism. Mitochondrial fractionation studies and quantitative electron microscopic immunocytochemistry revealed that most catalase was matrix-associated. Electrophoretic analysis and Western blotting of the mitochondrial matrix fraction indicated the presence of a protein with similar electrophoretic mobility to bovine and rat liver catalase and immunoreactive to anti-catalase antibody. Myocardial tissue has a lower catalase-specific activity and a greater mitochondrial H2O2 production/g of tissue than most organs. Thus catalase, representing 0.025% of heart mitochondrial protein, is important for detoxifying mitochondrial derived H2O2 and represents a key antioxidant defense mechanism for myocardial tissue.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Rat liver and heart mitochondria depend, in part, on catalase to reduce endogenous or exogenous hydrogen peroxide.
“Rat liver and heart mitochondria, however, depend, in part, on catalase to reduce endogenous or exogenous hydrogen peroxide (339, 369).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [339]
Cites
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
Biology of disease: free radicals and tissue injury.
Freeman, B. Α., & Jd, C. (1982) · PubMed · Cited by 3,059 · see citing works
Self-citationDawson, R. M. C. (1987) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(87)90411-7 · Cited by 2,961 · see citing works
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Turrens, J. F., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1910421 · Cited by 1,601 · see citing works
Self-citationDawson, R. M. C. (1987) · International Journal of Biochemistry · doi:10.1016/0020-711x(87)90251-5 · Cited by 1,299 · see citing works
Seligman, A. M., Karnovsky, M. J., Wasserkrug, H. L., & Hanker, J. S. (1968) · The Journal of Cell Biology · doi:10.1083/jcb.38.1.1 · Cited by 883 · see citing works
The oxidative inactivation of mitochondrial electron transport chain components and ATPase.
Zhang, Y., Marcillat, O., Giulivi, C., Ernster, L., & Davies, K. J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46227-2 · Cited by 713 · see citing works
Davies, K. J. A., & Doroshow, J. H. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35746-0 · Cited by 633 · see citing works
[57] Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
Boveris, A. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(84)05060-6 · Cited by 488 · see citing works
The effect of hyperoxia on superoxide production by lung submitochondrial particles
Turrens, J. F., Freeman, B. Α., Levitt, J. G., & Crapo, J. D. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90518-5 · Cited by 448 · see citing works
Self-citationHandbook of Methods for Oxygen Radical Research
Thomas, D. W. (1988) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1002/j.1536-4801.1988.tb09539.x · Cited by 444 · see citing works
Hyperoxia increases H2O2 release by lung mitochondria and microsomes
Turrens, J. F., Freeman, B. Α., & Crapo, J. D. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90519-7 · Cited by 337 · see citing works
Self-citationImmunolabeling for Electron Microscopy
Sarraf, C. (2000) · Methods in molecular medicine · doi:10.1385/1-59259-076-4:439 · Cited by 219 · see citing works
Viral membrane proteins acquire galactose in trans Golgi cisternae during intracellular transport
Griffiths, G. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.3.781 · Cited by 197 · see citing works
Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria.
Robinson, J. B. D., & Srere, P. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85153-0 · Cited by 168 · see citing works
Cytochrome c-catalyzed oxidation of organic molecules by hydrogen peroxide
Radí, R., Thomson, L., Rubbo, H., & Prodanov, E. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90171-e · Cited by 148 · see citing works
Marres, C. A. M., van Loon, A. P. G. M., Oudshoorn, P., STEEG, H. V., Grivell, L. A., & Slater, E. C. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb08731.x · Cited by 129 · see citing works
Cytochrome c-catalyzed membrane lipid peroxidation by hydrogen peroxide
Radí, R., Turrens, J. F., & Freeman, B. Α. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90172-f · Cited by 128 · see citing works
Self-citationGalaris, D., Cadenas, E., & Hochstein, P. E. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90509-2 · Cited by 110 · see citing works
Mechanisms of reoxygenation injury in myocardial infarction: Implications of a myoglobin redox cycle
Galaris, D., Eddy, L. J., Arduini, A., Cadenas, E., & Hochstein, P. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(89)80125-1 · Cited by 95 · see citing works
Mitochondrial lipid peroxidation by cumene hydroperoxide and its prevention by succinate
Bindoli, A., Cavallini, L., & Jocelyn, P. C. (1982) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(82)90192-x · Cited by 63 · see citing works
Localization of peroxidase activity inTrypanosoma cruzi microbodies
Docampo, R., de Boiso, J. F., Boveris, A. D., & Stoppani, A. O. M. (1976) · Cellular and Molecular Life Sciences · doi:10.1007/bf01933918 · Cited by 60 · see citing works
Evidence for the existence of catalase in the matrix space of rat‐heart mitochondria
Nohl, H., & HEGNER, D. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80537-7 · Cited by 54 · see citing works
The cytochrome c peroxidase activity of cytochrome oxidase.
Orii, Y. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34056-0 · Cited by 51 · see citing works
Role of catalase in metabolism of hydrogen peroxide by the perfused rat heart
THAYER, W. S. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80664-0 · Cited by 37 · see citing works
Sulfite oxidase from chicken liver
RITZMANN, M., & Bosshard, H. R. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09913.x · Cited by 5 · see citing works
Resistance of purified cholera toxin to enzymatic treatment with pancreatic elastase and papain
Antoni, G., Marsili, I., Tarli, P., et al. (1976) · Cellular and Molecular Life Sciences · doi:10.1007/bf01933917 · Cited by 2 · see citing works
Persistence of mitochondrial membrane potential of the heart cell under oxidative stress
Konno, N., Baba, A., Looper, K. J., et al. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90513-i · Cited by 2 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388 · see citing works
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
Self-citationMitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010 · see citing works
Production of Reactive Oxygen Species by Mitochondria
Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304854200 · Cited by 1,616 · see citing works
Potential Role of Carotenoids as Antioxidants in Human Health and Disease
Fiedor, J., & Burda, K. (2014) · Nutrients · doi:10.3390/nu6020466 · Cited by 1,420 · see citing works
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works
Mitochondria and reactive oxygen species
Kowaltowski, A. J., de Souza-Pinto, N. C., Castilho, R. F., & Vercesi, A. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.004 · Cited by 1,162 · see citing works
ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells
Snezhkina, A. V., Kudryavtseva, A. V., Kardymon, O. L., Savvateeva, M. V., Melnikova, N. V., Krasnov, G. S., & Dmitriev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6175804 · Cited by 934 · see citing works
Superoxide production by the mitochondrial respiratory chain
Turrens, J. F. (1997) · Bioscience Reports · doi:10.1023/a:1027374931887 · Cited by 903 · see citing works
Self-citationMitochondrial damage induced by conditions of oxidative stress
Kowaltowski, A. J., & Vercesi, A. E. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00216-0 · Cited by 866 · see citing works
Sivitz, W. I., & Yorek, M. A. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2531 · Cited by 742 · see citing works
The mitochondrial energy transduction system and the aging process
Navarro, A., & Boveris, A. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00213.2006 · Cited by 646 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
Nonn, L., Williams, R. R., Erickson, R. P., & Powis, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.3.916-922.2003 · Cited by 438 · see citing works
Chang, T.-S., Cho, C.-S., Park, S., Yu, S., Kang, S. W., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407707200 · Cited by 388 · see citing works
Manganese Superoxide Dismutase: Guardian of the Powerhouse
Holley, A. K., Bakthavatchalu, V., Velez-Roman, J. M., & St. Clair, D. K. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12107114 · Cited by 358 · see citing works
The Role of Reactive Oxygen Species in Mitochondrial Permeability Transition
Vercesi, A. E., Kowaltowski, A. J., Grijalba, M. T., Meinicke, A. R., & Castilho, R. F. (1997) · Bioscience Reports · doi:10.1023/a:1027335217774 · Cited by 325 · see citing works
Mitochondrial changes associated with glutathione deficiency
Meister, A. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00007-q · Cited by 242 · see citing works
Catalase Takes Part in Rat Liver Mitochondria Oxidative Stress Defense
Salvi, M., Battaglia, V., Brunati, A. M., La Rocca, N., Tibaldi, E., Pietrangeli, P., Marcocci, L., Mondovi, B., Rossi, C. A., & Toninello, A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701589200 · Cited by 231 · see citing works
Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene
Esposito, L. A., Kokoszka, J. E., Waymire, K. G., Cottrell, B., MacGregor, G. R., & Wallace, D. C. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00161-1 · Cited by 228 · see citing works
Respiration-dependent H2O2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system
Drechsel, D. A., & Patel, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101196 · Cited by 199 · see citing works
Aon, M. A., Stanley, B. A., Sivakumaran, V., Kembro, J. M., O'Rourke, B., Paolocci, N., & Cortassa, S. (2012) · Journal of General Physiology · doi:10.1085/jgp.201210772 · Cited by 200 · see citing works
Superoxide and Respiratory Coupling in Mitochondria of Insulin-Deficient Diabetic Rats
Herlein, J. A., Fink, B. D., O'Malley, Y., & Sivitz, W. I. (2009) · Endocrinology · doi:10.1210/en.2008-0404 · Cited by 77 · see citing works
The importance of mitochondrial DNA in aging and cancer
Desler, C., Marcker, M. L., Singh, K. K., & Rasmussen, L. J. (2011) · Journal of Aging Research · doi:10.4061/2011/407536 · Cited by 49 · see citing works
Long chain fatty acyl-CoA modulation of H2O2 release at mitochondrial complex I
Bortolami, S., Comelato, E., Zoccarato, F., Alexandre, A., & Cavallini, L. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9126-1 · Cited by 13 · see citing works
- Authors
- Radi, R., Turrens, J. F., Chang, L. Y., Bush, K. M., Crapo, J. D., & Freeman, B. A.
- Affiliations
- University of Alabama at Birmingham (US)
- ORCID
- Crapo, J.D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-11
- Volume
- 266
- Issue
- 32
- Pages
- 22028-22034
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1557712018
- Cited by
- 573
- References
- 28
- Citations by year
- 2026: 7 · 2025: 18 · 2024: 21 · 2023: 22 · 2022: 26 · 2021: 27 · 2020: 21 · 2019: 24 · 2018: 23 · 2017: 24 · 2016: 31 · 2015: 19 · 2014: 24 · 2013: 25 · 2012: 23
- FWCI
- 1.85
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl040458-05, 5r01ns024275-04, 5r01hl042609-08)
- National Heart, Lung, and Blood Institute (HL 42609, HL-40458)
- National Institute of Neurological Disorders and Stroke (NS24275)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
- Keywords
- catalase, heart mitochondria, hydrogen peroxide decomposition, antioxidant defense, myocardium, mitochondrial matrix, heme enzymes, cyanide inhibition, superoxide production, rats
- MeSH terms
- Animals, Catalase, Electron Transport Complex IV, Hydrogen Peroxide, Immunohistochemistry, Kinetics, Liver, Lung, Microbodies, Mitochondria, Mitochondria, Heart, Models, Biological, Molecular Weight, Myocardium, Oxygen Consumption, Microscopy, Immunoelectron, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review