Reactions of Bovine Liver Catalase with Superoxide Radicals and Hydrogen Peroxide
Abstract
The oxidized intermediates generated upon exposure of bovine liver catalase to hydrogen peroxide (H2O2) and superoxide radical (O2-) fluxes were examined with UV-visible spectrophotometry. H2O2 and O2- were generated by means of glucose/glucose oxidase and xanthine/xanthine oxidase systems. Serial overlay of absorption spectra in the Soret (350-450 nm) and visible (450-700 nm) regions showed that three oxidized intermediates, namely Compounds I, II and III, can be observed upon exposure of catalase to enzymatically generated H2O2 and O2-. Compound I is formed during the reaction of native enzyme with H2O2 and disappears in two ways: (i) via the catalytic reaction with H2O2 to restore native catalase and (ii) via the reaction with O2- to form Compound II. At low H2O2 concentrations (< 4.8 x 10(-9) M H2O2), Compound II reverts towards the native state mainly in a direct one-step reaction, whereas at higher H2O2 concentrations the pathway of Compound II back to the native enzyme involves Compound III. Formation of the latter from Compound II and H2O2 is irreversible and the rate constant of this reaction is 6.1 +/- 0.2 x 10(4) M-1 s-1. The formation of Compound III through the direct reaction of O2- with native enzyme has also been observed. Depending on the experimental conditions, the inactivation of catalase by O2- can be due to accumulation of Compound II ("slow" inhibition) or to the formation of Compound III ("rapid" inhibition) part of which leads to a dead end product. Formation of Compound III and of this dead end product are responsible for the irreversible inactivation in presence of an excess of H2O2.
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The catalase reaction proceeds in two steps: reduction of the first H2O2 molecule forms oxyferryl species (FeIVO), and the second H2O2 molecule reduces FeIVO to O2, H2O, and free enzyme.
“The reaction proceeds in two steps; the first step involves the reduction of the first molecule of H2O2 accompanied by the formation of oxyferryl species (FeIVO) and in the course of the second step, the FeIVO complex is reduced by the second molecule of H2O2 to O2, and H2O molecules and free enzyme (Lardinois 1995; Nandi et al. 2019)14and15”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Lardinois 1995
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- Authors
- Lardinois, O. M.
- Affiliations
- UCLouvain (BE)
- Corresponding author
- Lardinois, Olivier M.
- Venue
- Free Radical Research
- Publisher
- Informa UK Limited
- Published
- 1995-01
- Volume
- 22
- Issue
- 3
- Pages
- 251-274
- ISSN
- 1029-2470 (ISSN-L)
- 1071-5762
- OpenAlex
- W2149817242
- Cited by
- 91
- References
- 62
- Citations by year
- 2026: 2 · 2024: 3 · 2023: 4 · 2022: 4 · 2021: 1 · 2020: 1 · 2019: 6 · 2018: 2 · 2017: 3 · 2015: 2 · 2014: 3 · 2013: 3 · 2012: 4
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Research (publishedVersion)
- PubMed (publishedVersion)
- Digital Access to Libraries (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- catalase, superoxide, hydrogen peroxide, enzyme inactivation, irreversible inactivation, compound I, compound II, compound III, hydrogen peroxide catalysis, bovine liver
- MeSH terms
- Animals, Catalase, Cattle, Free Radicals, Hydrogen Peroxide, Liver
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