Cited by 573Redox biology and oxidative stressMitochondrial Function and PathologyCancer and biochemical research

Detection of catalase in rat heart mitochondria.

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Radi, R., Turrens, J.F., Chang, L.Y., Bush, K.M., Crapo, J.D., Freeman, B.A.·1991·Journal of Biological Chemistry

Abstract

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.

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Crossref · 10.1016/s0021-9258(18)54740-2

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  • 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]

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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)
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
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

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