Reaction of the Desulfoferrodoxin from Desulfoarculus baarsii with Superoxide Anion: EVIDENCE FOR A SUPEROXIDE REDUCTASE ACTIVITY *
TLDR
In this article, the authors showed that desulfoferrodoxin behaves as a superoxide reductase enzyme and thus provides new insights into the biological mechanisms designed for protection from oxidative stresses.About:
This article is published in Journal of Biological Chemistry.The article was published on 2000-01-07 and is currently open access. It has received 132 citations till now. The article focuses on the topics: Superoxide reductase activity & Superoxide reductase.read more
Citations
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Reactive oxygen species, antioxidants, and the mammalian thioredoxin system.
Jonas Nordberg,Elias S.J. Arnér +1 more
TL;DR: The TrxR-catalyzed regeneration of several antioxidant compounds, including ascorbic acid (vitamin C), selenium-containing substances, lipoic acid, and ubiquinone are summarized.
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Cellular Defenses against Superoxide and Hydrogen Peroxide
TL;DR: Bacteria comprise an exceptionally accessible experimental system that has provided many of the answers to the remaining puzzles in an anaerobic world, and current research seeks to identify these.
Journal ArticleDOI
Superoxide dismutases and superoxide reductases
Yuewei Sheng,Isabel A. Abreu,Diane E. Cabelli,Michael J. Maroney,Anne-Frances Miller,Miguel Teixeira,Joan Selverstone Valentine,Joan Selverstone Valentine +7 more
TL;DR: 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.
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Iron-sulphur clusters and the problem with oxygen.
TL;DR: The history of Fe‐S clusters is an unusual one that has profoundly shaped contemporary microbial ecology, and aerobes remain vulnerable to iron restriction and oxidative stress, features that higher organisms exploit in defending themselves against bacterial pathogens.
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Synthetic analogues of cysteinate-ligated non-heme iron and non-corrinoid cobalt enzymes
TL;DR: Making Low-Spin Co(III) More Reactive 840 3.2.1.
References
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
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Superoxide Dismutase AN ENZYMIC FUNCTION FOR ERYTHROCUPREIN (HEMOCUPREIN)
Joe M. McCord,Irwin Fridovich +1 more
TL;DR: The demonstration that O2·- can reduce ferricytochrome c and tetranitromethane, and that superoxide dismutase, by competing for the superoxide radicals, can markedly inhibit these reactions, is demonstrated.
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Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels☆
TL;DR: The staining procedure for localizing superoxide dismutase on polyacrylamide electrophoretograms has been applied to extracts obtained from a variety of sources and could thus be assayed either in crude extracts or in purified protein fractions.
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The inactivation of Fe-S cluster containing hydro-lyases by superoxide.
TL;DR: The working hypothesis is O2- inactivates these enzymes by oxidizing their clusters to an unstable oxidation state, and cluster degradation follows, and spinach dihydroxy-acid dehydratase, a member of the hydro-lyase class that has a catalytically active [2Fe-2S] cluster, is not inactivated and does not lose iron in the presence of O2.