Identification of Iron(III) Peroxo Species in the Active Site of the Superoxide Reductase SOR from Desulfoarculus baarsii
Abstract
The active site of superoxide reductase SOR consists of an Fe 2+ center in an unusual [His 4 Cys 1 ] square-pyramidal geometry. It specifically reduces superoxide to produce H 2 O 2 . Here, we have reacted the SOR from Desulfoarculus baarsii directly with H 2 O 2 . We have found that its active site can transiently stabilize an Fe 3+ -peroxo species that we have spectroscopically characterized by resonance Raman. The mutation of the strictly conserved Glu47 into alanine results in a stabilization of this Fe 3+ -peroxo species, when compared to the wild-type form. These data support the hypothesis that the reaction of SOR proceeds through such a Fe 3+ -peroxo intermediate. This also suggests that Glu47 might serve to help H 2 O 2 release during the reaction with superoxide.
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UV-visible spectroscopy has been applied to study the catalytic activity of SOR.
“UV-visible spectroscopy has been applied to study the catalytic activity of SOR [92,93,94,95,96,97,98,99].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [95]
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Superoxide dismutases and superoxide reductases
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Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
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- Authors
- Mathé, C., Mattioli, T. A., Horner, O., Lombard, M., Latour, J.-M., Fontecave, M., & Nivière, V.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Nivière, Vincent
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-04-11
- Volume
- 124
- Issue
- 18
- Pages
- 4966-4967
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2964323342
- Cited by
- 116
- References
- 9
- Citations by year
- 2024: 2 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 3 · 2016: 4 · 2015: 2 · 2014: 7 · 2013: 2 · 2012: 5
- FWCI
- 9.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the American Chemical Society (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- superoxide reductase, active site, hydrogen peroxide release, superoxide reduction, resonance Raman spectroscopy, enzyme mechanism, peroxo intermediate
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