H2O2 detection from intact mitochondria as a measure for one-electron reduction of dioxygen requires a non-invasive assay system11Dedicated to Prof. E. Elstner, on the occasion of his 60th anniversary.
Open accessAbstract
Evaluation of the existence of superoxide radicals (O*-(2)), the site of generation and conditions required for one-e(-) transfer to oxygen from biological redox systems is a prerequisite for the understanding of the deregulation of O(2) homeostasis leading to oxidative stress. Mitochondria are increasingly considered the major O*-(2) source in a great variety of diseases and the aging process. Contradictory reports on mitochondrial O*-(2) release prompted us to critically investigate frequently used O*-(2) detection methods for their suitability. Due to the impermeability of the external mitochondrial membrane for most constituents of O*-(2) detection systems we decided to follow the stable dismutation product H(2)O(2). This metabolite was earlier shown to readily permeate into the cytosol. With the exception of tetramethylbenzidine none of the chemical reactants indicating the presence of H(2)O(2) by horseradish peroxidase-catalyzed absorbance change were suited due to solubility problems or low extinction coefficients. Tetramethylbenzidine-dependent H(2)O(2) detection was counteracted by rereduction of the dye through e(-) carriers of the respiratory chain. Although the fluorescent dyes scopoletin and homovanillic acid were found to be suited for the detection of mitochondrial H(2)O(2) release, fluorescence change was strongly affected by mitochondrial protein constituents. The present study has resolved this problem by separating the detection system from H(2)O(2)-producing mitochondria.
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Incomplete reduction of molecular oxygen to superoxide occurs as a result of electron leak during normal respiration in mitochondrial electron transport chain complexes or by enzymatic reduction of molecular oxygen.
“This incomplete reduction reaction occurs as a result of electron leak during normal respiration in the mitochondrial electron transport chain (ETC) complexes or by enzymatic reduction of molecular oxygen (249, 399).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [399]
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- Authors
- Staniek, K., & Nohl, H.
- Affiliations
- University of Veterinary Medicine Vienna (AT)
- Corresponding author
- Nohl, Hans
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 1999-10
- Volume
- 1413
- Issue
- 2
- Pages
- 70-80
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W1602920781
- Cited by
- 124
- References
- 28
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 1 · 2019: 5 · 2018: 3 · 2017: 2 · 2016: 2 · 2015: 5 · 2014: 3 · 2013: 9 · 2012: 3
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- 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
- hydrogen peroxide detection, superoxide, tetramethylbenzidine, horseradish peroxidase, scopoletin, homovanillic acid, fluorescent probes, oxidative stress, oxygen homeostasis
- MeSH terms
- Animals, Antimycin A, Benzidines, Catalase, Fluorescent Dyes, Homovanillic Acid, Hydrogen Peroxide, Intracellular Membranes, Male, Methacrylates, Mitochondria, Mitochondria, Heart, Oxidation-Reduction, Oxygen, Scopoletin, Spectrometry, Fluorescence, Spectrophotometry, Superoxides, Thiazoles, Rats, Sprague-Dawley, Rats
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