Redox

About: Redox is a research topic. Over the lifetime, 26853 publications have been published within this topic receiving 862368 citations. The topic is also known as: reduction-oxidation & reduction-oxidation reaction.

How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis

Abstract: The orbital structure of molecular oxygen constrains it to accept electrons one at a time, and its unfavourable univalent reduction potential ensures that it can do so only with low-potential redox partners. In E. coli, this restriction prevents oxygen from oxidizing structural molecules. Instead, it primarily oxidizes reduced flavins, a reaction that is harmful only in that it generates superoxide and hydrogen peroxide as products. These species are stronger oxidants than is oxygen itself. They can oxidize dehydratase iron-sulphur clusters and sulphydryls, respectively, and thereby inactivate enzymes that are dependent upon these functional groups. Hydrogen peroxide also oxidizes free iron, generating hydroxyl radicals. Because hydroxyl radicals react with virtually any biomolecules they encounter, their reactivity is broadly dissipated, and only their reactions with DNA are known to have an important physiological impact. E. coli elaborates scavenging and repair systems to minimize the impact of this adventitious chemistry; mutants that lack these defences grow poorly in aerobic habitats. Some of the growth deficits of these mutants cannot be easily ascribed to sulphydryl, cluster, or DNA damage, indicating that important aspects of oxidative stress still lack a biochemical explanation. Obligate anaerobes cannot tolerate oxygen because they utilize metabolic schemes built around enzymes that react with oxidants. The reliance upon low-potential flavoproteins for anaerobic respiration probably causes substantial superoxide and hydrogen peroxide to be produced when anaerobes are exposed to air. These species then generate damage of the same type that they produce in aerotolerant bacteria. However, obligate anaerobes also utilize several classes of dioxygen-sensitive enzymes that are not needed by aerobes. These enzymes are used for processes that help maintain the redox balance during anaerobic fermentations. They catalyse reactions that are chemically difficult, and the reaction mechanisms require the solvent exposure of radicals or low-potential metal clusters that can react rapidly with oxygen. Recent work has uncovered adaptive strategies by which obligate anaerobes seek to minimize the damage done by superoxide and hydrogen peroxide. Their failure to divest themselves of enzymes that can be directly damaged by molecular oxygen suggests that evolution has not yet provided economical options to them.

Peroxide processing in photosynthesis: antioxidant coupling and redox signalling.

Abstract: Photosynthesis has a high capacity for production of hydrogen peroxide (H2O2), but the intracellular levels of this relatively weak oxidant are controlled by the antioxidant system, comprising a network of enzymatic and non-enzymatic components that notably includes reactions linked to the intracellular ascorbate and glutathione pools. Mutants and transformed plants with specific decreases in key components offer the opportunity to dissect the complex system that maintains redox homeostasis. Since H2O2 is a signal-transducing molecule relaying information on intracellular redox state, the pool size must be rigorously controlled within each compartment of the cell. This review focuses on compartment-specific differences in the stringency of redox coupling between ascorbate and glutathione, and the significance this may have for the flexibility of the control of gene expression that is linked to photosynthetic H2O2 production.

Electrochemical Oxidation of Quercetin

Abstract: The mechanism of electrochemical oxidation of quercetin on a glassy carbon electrode has been studied using cyclic, differential pulse and square-wave voltammetry at different pH. It proceeds in a cascade mechanism, related with the two catechol hydroxyl groups and the other three hydroxyl groups which all present electroactivity, and the oxidation is pH dependent. Quercetin also adsorbs strongly on the electrode surface; and the final oxidation product is not electroactive and blocks the electrode surface. The oxidation of the catechol 3,4-dihydroxyl electron-donating groups, occurs first, at very low positive potentials, and is a two electron two proton reversible reaction. The hydroxyl group oxidized next was shown to undergo an irreversible oxidation reaction, and this hydroxyl group can form a intermolecular hydrogen bond with the neighboring oxygen. The other two hydroxyl groups also have an electron donating effect and their oxidation is reversible.