Discovery of superoxide reductase: an historical perspective

  title={Discovery of superoxide reductase: an historical perspective},
  author={Vincent Nivi{\`e}re and Marc Fontecave},
  journal={JBIC Journal of Biological Inorganic Chemistry},
For more than 30 years, the only enzymatic system known to catalyze the elimination of superoxide was superoxide dismutase, SOD. SOD has been found in almost all organisms living in the presence of oxygen, including some anaerobic bacteria, supporting the notion that superoxide is a key and general component of oxidative stress. Recently, a new concept in the field of the mechanisms of cellular defense against superoxide has emerged. It was discovered that elimination of superoxide in some… 
Understanding the Mechanism of Superoxide Reductase Promoted Reduction of Superoxide
Superoxide reductases (SORs) are nonheme, iron-containing enzymes which reduce superoxide (O2 ‐ ) to hydrogen peroxide (H2O2) in anaerobic organisms. In contrast to the classical superoxide
Superoxide Dismutases and Superoxide Reductases
The SORs and three very different types of SOD enzymes are redox-active metalloenzymes that have evolved entirely independently from one another for the purpose of lowering superoxide concentrations, suggesting that, from the start of the rise of O2 on Earth, the chemistry of superoxide has been an important factor during evolution.
Enzymatic Antioxidant Systems in Early Anaerobes: Theoretical Considerations.
The results presented here suggest that the last universal common ancestor (LUCA) was not a strict anaerobe, and that O2 could have been available for the first microorganisms before oxygenic photosynthesis evolved from the intrinsic activity of EAS, not solely from abiotic sources.
Superoxide reductase from Giardia intestinalis: structural characterization of the first SOR from a eukaryotic organism shows an iron centre that is highly sensitive to photoreduction.
Superoxide reductase (SOR), which is commonly found in prokaryotic organisms, affords protection from oxidative stress by reducing the superoxide anion to hydrogen peroxide. The reaction is catalyzed
Comparative electrochemical study of superoxide reductases
A comparison of the redox potentials and redox behavior of all the proteins is presented, and the results show that SOR center II is thermodynamically more stable than similar centers in different proteins, which may be related to an intramolecular electron transfer function.
Detoxification of superoxide without production of H2O2: Antioxidant activity of superoxide reductase complexed with ferrocyanide
In vivoexperiments showed that formation of the SOR–ferrocyanide complex increased the antioxidant capabilities of SOR expressed in an Escherichia coli sodA sodB recA mutant strain, describing an unprecedented O2·̅ detoxification activity, catalyzed by the S OR–ferron redox complex, which does not conduct to the production of the toxic H2O2 species.
Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases
It is demonstrated that, in Dg, another iron–sulfur protein, a desulforedoxin, is able to transfer electrons to SOR more efficiently than rubredoxin, and was then assigned as the potential physiological electron donor in this organism.
Mimicking SOD, Why and How: Bio-Inspired Manganese Complexes as SOD Mimic
This chapter will focus on the SOD physicochemical parameters valuable for the chemical design of low-molecular-weight compounds displaying superoxide scavenging activity and the approaches developed by chemists following the footsteps of Nature for this purpose.


Superoxide reductase: fact or fiction?
The available spectroscopic and structural information provide a convincing case that the catalytic Fe site of SOR is structurally and electronically tuned to mediate superoxide reduction rather than oxidation, and the role of otherwise well-characterized proteins like rubrerythrin, NADH peroxidase, and rubredoxin:oxygen oxidoreductase in "anaerobic" oxygen metabolism has yet to be established.
The mechanism(s) of superoxide reduction by superoxide reductases in vitro and in vivo
This Commentary addresses the mechanism of superoxide reduction catalyzed by this unique active site in SORs both in vitro and in vivo.
What biological purpose is served by superoxide reductase?
  • J. Imlay
  • Physics
    JBIC Journal of Biological Inorganic Chemistry
  • 2002
Most physical, distributional, and genetic data suggest that the SOR activity of oxygen-sensitive microbes contain superoxide reductase (SOR) activity, and that their role is indeed to scavenge superoxide.
What is the ultimate fate of superoxide anion in vivo?
The role of these enzymes and their biological relationship to the well-known superoxide dismutases is discussed and they are shown to be physiologically competent at removing superoxide.
Superoxide scavenging by neelaredoxin: dismutation and reduction activities in anaerobes
The experimental evidence for the activity of these proteins as superoxide dismutases or as donor:superoxide oxidoreductases is discussed in this Commentary, giving particular emphasis to the neelaredoxin from the hyperthermophilic archaeon Archaeoglobusfulgidus.
Anaerobic microbes: oxygen detoxification without superoxide dismutase.
Unlike superoxide dismutase, the enzyme that protects aerobes from the toxic effects of oxygen, SOR does not catalyze the production of oxygen from superoxide and therefore confers a selective advantage on anaerobes.
Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states.
The structures of the oxidized and reduced forms of SOR suggest a mechanism by which superoxide accessibility may be controlled and define a possible binding site for rubredoxin, the likely physiological electron donor to SOR.
Superoxide reductase as a unique defense system against superoxide stress in the microaerophile Treponema pallidum.
A gene in T. pallidum is described with sequence homologies to a new class of antioxidant systems, named superoxide reductases, recently isolated from sulfate-reducing bacteria, and the question of the importance of superoxide reductionases in mechanisms for detoxifying superoxide radicals is raised.
Modeling the reactivity of superoxide reducing metalloenzymes with a nitrogen and sulfur coordinated iron complex.
The synthesis and structure of a five-coordinate Fe(II) complex, [FeIISMe2N4 (tren)](PF6) (1), which models the reactive properties of SORs, is reported, and the thiolate ligand appears to play an important role in promoting SOR activity.