Superoxide reduction by Nanoarchaeum equitans neelaredoxin, an enzyme lacking the highly conserved glutamate iron ligand
Abstract
Superoxide reductases (SORs) are antioxidant enzymes present in many prokaryotes, either anaerobes or microaerophiles, which detoxify superoxide by reducing it to hydrogen peroxide. The reaction mechanism involves the diffusion-limited encounter of superoxide with the reduced iron site and concomitant formation of an Fe(3+)-(hydro)peroxo adduct that, upon protonation, leads to the formation of hydrogen peroxide. By the end of this process, a glutamate residue coordinates the ferric ion, acting as a sixth ligand. Although this residue is able to shuttle protons to the intermediate at low pH, it seems to have a minor relevance to the overall reduction mechanism. Nevertheless, this ligand is conserved in most SORs known thus far, with the notable exception of neelaredoxin from Nanoarchaeum equitans. The protein of this organism was cloned and overexpressed, and its spectroscopic characterization revealed distinct pH-equilibrium properties in comparison with those of glutamate-containing SORs. A three-dimensional model of this protein was generated in an effort to identify structural properties that could explain these distinct features. Pulse radiolysis measurements showed that the efficiency of this enzyme in reducing superoxide is comparable to that of glutamate-containing SORs, thus definitely ruling out the requirement for such a ligand in the reduction mechanism.
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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 [94]
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- Authors
- Rodrigues, J. V., Victor, B. L., Huber, H., Saraiva, L. M., Soares, C. M., Cabelli, D. E., & Teixeira, M.
- Affiliations
- Universidade Nova de Lisboa (PT)
- University of Regensburg (DE)
- Brookhaven National Laboratory (US)
- Corresponding author
- Teixeira, Miguel
- Venue
- JBIC Journal of Biological Inorganic Chemistry
- Published
- 2007-10-30
- Volume
- 13
- Issue
- 2
- Pages
- 219-228
- ISSN
- 0949-8257 (ISSN-L)
- 1432-1327
- OpenAlex
- W2081567909
- Cited by
- 24
- References
- 51
- Citations by year
- 2023: 1 · 2020: 1 · 2019: 2 · 2018: 1 · 2016: 1 · 2015: 1 · 2014: 5 · 2013: 1 · 2012: 1
- FWCI
- 1.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- JBIC Journal of Biological Inorganic Chemistry (publishedVersion)
- PubMed (publishedVersion)
- University of Regensburg Publication Server (University of Regensburg) (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- superoxide reductase, Nanoarchaeum equitans, superoxide reduction, hydrogen peroxide production, pulse radiolysis, protein structure modeling, antioxidant enzymes, anaerobic archaea
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Electron Spin Resonance Spectroscopy, Iron, Ligands, Models, Molecular, Molecular Sequence Data, Mutation, Oxidation-Reduction, Spectrophotometry, Ultraviolet, Superoxides, Superoxide Dismutase, Sequence Alignment, Conserved Sequence, Protein Structure, Secondary, Glutamic Acid, Sequence Analysis, Protein, Iron-Binding Proteins, Nanoarchaeota
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