Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: Comparison with neelaredoxin

Rodrigues, João V.; Saraiva, Lígia M.; Abreu, Isabel A.; Teixeira, Miguel; Cabelli, Diane E.

doi:10.1007/s00775-006-0182-x

Cited by 40Metal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteinsEnzyme Structure and Function

Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: Comparison with neelaredoxin

Rodrigues, João V., Saraiva, Lígia M., Abreu, Isabel A., Teixeira, Miguel, Cabelli, Diane E.·2007·JBIC Journal of Biological Inorganic Chemistry

DOI 10.1007/s00775-006-0182-x

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Abstract

Superoxide reductases (SORs) are non-heme iron-containing enzymes that remove superoxide by reducing it to hydrogen peroxide. The active center of SORs consists of a ferrous ion coordinated by four histidines and one cysteine in a square-pyramidal geometry. In the 2Fe-SOR, a distinct family of SORs, there is an additional desulforedoxin-like site that does not appear to be involved in SOR activity. Our previous studies on recombinant Archaeoglobus fulgidus neelaredoxin (1Fe-SOR) have shown that the reaction with superoxide involves the formation of a transient ferric form that, upon protonation, decays to yield an Fe(3+)-OH species, followed by binding of glutamate to the ferric ion via replacement of hydroxide (Rodrigues et al. in Biochemistry 45:9266-9278, 2006). Here, we report the characterization of recombinant desulfoferrodoxin from the same organism, which is a member of the 2Fe-SOR family, and show that the steps involved in the superoxide reduction are similar in both families of SOR. The electron donation to the SOR from its redox partner, rubredoxin, is also presented here.

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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 [93]

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Authors: Rodrigues, J. V., Saraiva, L. M., Abreu, I. A., Teixeira, M., & Cabelli, D. E.
Affiliations: Instituto de Tecnologia Química e Biológica António Xavier (PT)
Brookhaven National Laboratory (US)
Corresponding author: Teixeira, Miguel
ORCID: Rodrigues, João V.
Abreu, Isabel A.
Teixeira, Miguel
Venue: JBIC Journal of Biological Inorganic Chemistry
Publisher: Springer Science and Business Media LLC
Published: 2006-10-26
Volume: 12
Issue: 2
Pages: 248-256
ISSN: 0949-8257 (ISSN-L)
1432-1327
DOI: 10.1007/s00775-006-0182-x
OpenAlex: W1997295152
Cited by: 40
References: 39
Citations by year: 2025: 1 · 2024: 1 · 2023: 2 · 2020: 1 · 2019: 1 · 2018: 1 · 2016: 3 · 2015: 2 · 2014: 4 · 2013: 1 · 2012: 2
FWCI: 2.83
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: JBIC Journal of Biological Inorganic Chemistry (publishedVersion)
PubMed (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, Archaeoglobus fulgidus, superoxide reduction, non-heme iron enzymes, rubredoxin, electron transfer, hydrogen peroxide
MeSH terms: Bacterial Proteins, Ferredoxins, Hydrogen Peroxide, Models, Molecular, Oxidation-Reduction, Oxidoreductases, Recombinant Proteins, Rubredoxins, Superoxides, Superoxide Dismutase, Nonheme Iron Proteins, Archaeoglobus fulgidus, Iron-Binding Proteins

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Superoxide reduction by Archaeoglobus fulgidus desulfoferrodoxin: Comparison with neelaredoxin

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