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.

Elements of Molecular and Biomolecular Electrochemistry: An Electrochemical Approach to Electron Transfer Chemistry

Abstract: Preface. Chapter 1. Single Electron Transfer at an Electrode. 1.1 Introduction. 1.2 Cyclic Voltammetry of Fast Electron Transfers. 1.3 Technical Aspects. 1.4 Electron Transfer Kinetics. 1.5 Successive One-Electron Transfers vs. Two-Electron Transfers. References and Notes. Chapter 2. Coupling of Electrode Electron Transfers with Homogeneous Chemical Reactions. 2.1 Introduction. 2.2 Establishing the Mechanisms and Measuring the Rate Constants for Homogeneous Reactions by Means of Cyclic Voltammetry and Potential Step Chronoamperometry. 2.3 Application of Redox Catalysis to the Kinetic Characterization of Fast Follow-up Reactions. 2.4 Product Distribution in Preparative Electrolysis. 2.5 Chemical Classification and Examples. 2.6 Redox Properties of Transient Radicals. 2.7 Electrochemistry as a Trigger for Radical Chemistry or Ionic Chemistry. References and Notes. Chapter 3. Electron Transfer, Bond Breaking, and Bond Formation. 3.1 Introduction. 3.2 Dissociative Electron Transfer. 3.3 Interactions Between Fragments in the Product Cluster. 3.4 Stepwise vs. Concerted Mechanisms. 3.5 Cleavage of Ion Radicals. Reactions of Radicals with Nucleophiles. 3.6 Role of Solvent in Ion-radical Cleavage and in Stepwise vs. Concerted Competitions. 3.7 Dichotomy and Connections between SN2 Reactions and Dissociative Electron Transfers. References and Notes. Chapter 4. Molecular catalysis of Electrochemical Reactions. 4.1 Introduction. 4.2 Homogeneous Molecular Catalysis. 4.3 Supported Molecular catalysis (Immobilized catalysts). References and Notes. Chapter 5. Enzymatic Catalysis of Electrochemical Reactions. 5.1 Introduction. 5.2 Homogeneous Enzymatic Catalysis. 5.3 Immobilized Enzymes in Monomolecular Layers. 5.4 Spatially Ordered Multimonomolecular Layered Enzyme coatings. References and Notes. Chapter 6. Appendixes. 6.1 Single Electron Transfer at an Electrode. 6.2 Coupling of Homogeneous Chemical Reactions with Electron transfer. 6.3 Electron Transfer, Bond Breaking, and Bond Formation. 6.4 Analysis of Supported Molecular catalysis by Rotating Disk Electrode Voltammetry. 6.5 Enzymatic catalysis Responses. References and Notes. Glossary of Symbols. Index.

Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer.

Abstract: The cellular glutathione redox buffer is assumed to be part of signal transduction pathways transmitting environmental signals during biotic and abiotic stress, and thus is essential for regulation of metabolism and development. Ratiometric redox-sensitive GFP (roGFP) expressed in Arabidopsis thaliana reversibly responds to redox changes induced by incubation with H(2)O(2) or DTT. Kinetic analysis of these redox changes, combined with detailed characterization of roGFP2 in vitro, shows that roGFP2 expressed in the cytosol senses the redox potential of the cellular glutathione buffer via glutaredoxin (GRX) as a mediator of reversible electron flow between glutathione and roGFP2. The sensitivity of roGFP2 toward the glutathione redox potential was tested in vivo through manipulating the glutathione (GSH) content of wild-type plants, through expression of roGFP2 in the cytosol of low-GSH mutants and the endoplasmic reticulum (ER) of wild-type plants, as well as through wounding as an example for stress-induced redox changes. Provided the GSH concentration is known, roGFP2 facilitates the determination of the degree of oxidation of the GSH solution. Assuming sufficient glutathione reductase activity and non-limiting NADPH supply, the observed almost full reduction of roGFP2 in vivo suggests that a 2.5 mm cytosolic glutathione buffer would contain only 25 nm oxidized glutathione disulfide (GSSG). The high sensitivity of roGFP2 toward GSSG via GRX enables the use of roGFP2 for monitoring stress-induced redox changes in vivo in real time. The results with roGFP2 as an artificial GRX target further suggest that redox-triggered changes of biologic processes might be linked directly to the glutathione redox potential via GRX as the mediator.

The Redox Code

Abstract: Significance: The redox code is a set of principles that defines the positioning of the nicotinamide adenine dinucleotide (NAD, NADP) and thiol/disulfide and other redox systems as well as the thiol redox proteome in space and time in biological systems. The code is richly elaborated in an oxygen-dependent life, where activation/deactivation cycles involving O2 and H2O2 contribute to spatiotemporal organization for differentiation, development, and adaptation to the environment. Disruption of this organizational structure during oxidative stress represents a fundamental mechanism in system failure and disease. Recent Advances: Methodology in assessing components of the redox code under physiological conditions has progressed, permitting insight into spatiotemporal organization and allowing for identification of redox partners in redox proteomics and redox metabolomics. Critical Issues: Complexity of redox networks and redox regulation is being revealed step by step, yet much still needs to be lea...