Keywords:
Cytology.
;
Electronic books.
Type of Medium:
Online Resource
Pages:
1 online resource (387 pages)
Edition:
1st ed.
ISBN:
9783319440811
URL:
https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=4692911
Language:
English
Note:
Intro -- Preface -- ReferencesCorpas FJ, Gupta DK, Palma JM (2015) Production sites of reactive oxygen species (ROS) in plants. In: Gupta DK, Palma JM, Corpas FJ (eds) Reactive oxygen species and oxidative damage in plants under stress. Springer Publication, Germany, p 1-22Gupta DK, Corpas FJ, Palma JM (2013) Heavy metal stress in plants. Springer-Verlag, GermanyGupta DK, Palma JM, Corpas FJ (2015) Reactive oxygen species and oxidative damage in plants under stress. Springer-Verlag, GermanyGupta DK, Peña LB, Romero -- Contents -- About the Editors -- 1 Cellular Redox Homeostasis as Central Modulator in Plant Stress Response -- Abstract -- 1.1 Introduction -- 1.2 ROS Production Pathways -- 1.3 ROS-Scavenging Mechanisms -- 1.3.1 Non-enzymatic Antioxidants and Ascorbate-Glutathione Cycle -- 1.3.2 ROS Removal Enzymes -- 1.4 Redox-Dependent Signalling -- 1.4.1 Redox Signalling in Different Cell Compartments -- 1.4.2 The Role of Redox-Sensitive Proteins in Signal Transduction -- 1.5 Conclusion and Perspectives -- References -- 2 Plant Cell Redox Homeostasis and Reactive Oxygen Species -- Abstract -- 2.1 The Concept of Redox Homeostasis in Plants -- 2.2 Production of Reactive Oxygen Species -- 2.2.1 Types of ROS -- 2.2.1.1 Singlet Oxygen -- 2.2.1.2 Superoxide Radical -- 2.2.1.3 Hydrogen Peroxide -- 2.2.1.4 Hydroxyl Radical -- 2.3 ROS Detoxification in Plants -- 2.3.1 Enzymatic Antioxidants -- 2.3.2 Non-enzymatic Antioxidants -- 2.4 Conclusion -- References -- 3 Redox Balance in Chloroplasts as a Modulator of Environmental Stress Responses: The Role of Ascorbate Peroxidase and Nudix Hydrolase in Arabidopsis -- Abstract -- 3.1 Introduction -- 3.2 Ascorbate-Dependent Redox System in Chloroplasts -- 3.2.1 Chloroplastic APX and its Contribution to Redox Modulation -- 3.2.2 Recycling of Ascorbate and Glutathione.
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3.3 Roles of Nudix Hydrolases in the Regulation of the Redox State in Chloroplasts -- 3.4 Conclusion -- Acknowledgments -- References -- 4 Physiological Processes Contributing to the Synthesis of Ascorbic Acid in Plants -- Abstract -- 4.1 Introduction -- 4.2 AA Synthesis in Plant Tissues -- 4.3 Environmental Regulation of AA Synthesis in Plant Tissues -- 4.3.1 The Light Control of AA Synthesis -- 4.4 Physiological Processes Affecting AA Synthesis -- 4.4.1 Feedback Regulation and Other Specific Regulators -- 4.4.1.1 Relationship of AA Synthesis with Plant Metabolism -- Interaction with Photosynthesis -- Interaction with Respiration -- Regulation of AA Synthesis by Plant Hormones -- 4.5 The Synthesis of AA in Fruits -- 4.5.1 The Effect of Light on the Synthesis of AA in Fruit -- 4.6 The Changes of AA During Plant Domestication -- 4.7 Concluding Remark -- Acknowledgments -- References -- 5 Redox State in Plant Mitochondria and its Role in Stress Tolerance -- Abstract -- 5.1 Introduction -- 5.2 NADP in the Mitochondrial Matrix -- 5.3 Isocitrate Dehydrogenase Substrate Cycle -- 5.4 Glycolytic Reactions Associated with Plant Mitochondria -- 5.5 Malate and Citrate Valves -- 5.6 Modulation of Redox State in Mitochondria by Thioredoxin -- 5.7 Ascorbate and Glutathione -- 5.8 Production of Reactive Oxygen Species by Plant Mitochondria -- 5.9 Generation of Nitric Oxide by Plant Mitochondria -- 5.10 Cross Talk Between NO and ROS -- 5.11 Mitochondrial ROS and NO Production in Stress Response -- 5.12 Conclusion -- References -- 6 Oxidative Stress and its Role in Peroxisome Homeostasis in Plants -- Abstract -- 6.1 Introduction -- 6.2 Reactive Oxygen Species in Plants -- 6.3 ROS Generation and Elimination in Plant Cells -- 6.3.1 ROS Generation in Peroxisomes -- 6.3.1.1 Photorespiration -- 6.3.1.2 β-Oxidation of Fatty Acids -- 6.3.1.3 Other Pathways.
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6.3.2 ROS Damage and the Scavenging Antioxidant System in Peroxisomes -- 6.3.2.1 The Destructive Effect of ROS -- 6.3.2.2 Peroxisomal ROS Scavenging System -- 6.4 Redox Regulation of Peroxisome Biogenesis -- 6.4.1 Peroxisome Biogenesis -- 6.4.2 The Import of Peroxisomal Matrix Proteins -- 6.4.3 Oxidative Stress Represses Peroxisome Biogenesis -- 6.4.3.1 Oxidative Stress Represses Peroxisomal Matrix Protein Import -- 6.4.3.2 Oxidative Stress Affects the Subcellular Localization and Activity of Peroxisomal Proteins -- 6.4.3.3 Oxidative Stress Affects Peroxisomal Proliferation -- 6.5 Redox State Regulates Peroxisome Degradation -- 6.5.1 Pexophagy is the Main Way to Degrade Oxidized Peroxisomes -- 6.5.2 Pexophagy Involved in Peroxisome Remodeling -- 6.6 Conclusion -- Acknowledgments -- References -- 7 Glutathione-Related Enzyme System: Glutathione Reductase (GR), Glutathione Transferases (GSTs) and Glutathione Peroxidases (GPXs) -- Abstract -- 7.1 Introduction -- 7.2 Glutathione -- 7.3 Glutathione Reductase Supports Continuous Reduction of the Oxidized Glutathione -- 7.4 GSTs are a Large and Even Broadening Family of Proteins Which Comprise Highly Heterogenic Enzymes with Diverse Structure and Function -- 7.5 Glutathione Peroxidase may be a Link Between Glutathione and Thioredoxin Systems -- 7.6 GSH-Related Enzymes and the Redox-Dependent Signaling -- 7.7 Concluding Remark -- Acknowledgments -- References -- 8 Glutathione Metabolism in Plants Under Metal and Metalloid Stress and its Impact on the Cellular Redox Homoeostasis -- Abstract -- 8.1 Soil Toxic Elements and the Particular Cases of Mercury and Arsenic -- 8.2 Oxidative Stress and Plant Tolerance to Toxic Metal(loid)s -- 8.3 Glutathione is a Key Component of the Antioxidant Response to Toxic Metal(loid)s -- 8.4 Toxic Element Binding to Biothiols is Essential for Plant Tolerance.
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8.5 Regulation of Glutathione Metabolism Under Metal(loid) Stress -- 8.5.1 Endogenous Factors that Modulate the Biothiol Metabolism -- 8.6 Metallomics to Characterize Biothiols Metabolism and Metal Speciation -- 8.7 Phytoremediation of Toxic Elements in Perspective -- 8.8 Concluding Remark -- Acknowledgments -- References -- 9 Glutathione and Related Enzymes in Response to Abiotic Stress -- Abstract -- 9.1 Introduction -- 9.2 The Role of GSH and Related Enzymes in Plant Response to Different Abiotic Stressors -- 9.2.1 Drought -- 9.2.2 Temperature -- 9.2.3 Salinity -- 9.2.4 Heavy Metals -- 9.2.5 Herbicides -- 9.3 Conclusion -- References -- 10 The Function of Cellular Redox Homeostasis and Reactive Oxygen Species (ROS) in Plants Tolerance to Abiotic Stresses -- Abstract -- 10.1 Introduction -- 10.2 Source of ROS and Redox Homeostasis in Plants -- 10.2.1 ROS Generation and Redox Homeostasis in Chloroplast -- 10.2.2 ROS Generation and Redox Homeostasis in Mitochondria -- 10.2.3 ROS Generation and Redox Homeostasis in Peroxisome -- 10.3 Cross Talk Between ROS and Signal Molecular in Regulating Plant Tolerance to Abiotic Stress -- 10.3.1 ROS and ABA -- 10.3.2 ROS and Nitric Oxide -- 10.3.3 ROS and Calcium -- 10.3.4 ROS and Other Signal Molecules -- 10.4 Summary and Perspective -- References -- 11 Abiotic Stress-Induced Redox Changes and Programmed Cell Death in Plants-A Path to Survival or Death? -- Abstract -- 11.1 Introduction -- 11.2 Role of ROS in Abiotic Stress-Induced PCD in Plants -- 11.3 High-Light-Induced PCD -- 11.4 Ultraviolet (UV)- and Ozone-Mediated PCD -- 11.5 PCD Induced by Heavy Metals -- 11.6 Temperature-Induced PCD -- 11.7 Salinity Stress-Associated PCD -- 11.8 Role and Interaction of Mitochondria and Plastids in PCD -- 11.9 Concluding Remark -- References.
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12 The Role of ROS and Redox Signaling During the Initial Cellular Response to Abiotic Stress -- Abstract -- 12.1 Introduction -- 12.2 ROS-Signaling During Light Acclimation and High-Light Stress -- 12.2.1 Sources of Chloroplastic ROS Production -- 12.2.2 ROS-Dependent Chloroplast-to-Nucleus Signaling Pathways -- 12.3 ROS-Mediated Signaling Events During Temperature Stress -- 12.3.1 ROS Burst During Temperature Stress -- 12.3.2 ROS-Mediated Signaling Cascades During Temperature Stress -- 12.4 ROS-Dependent Salt Stress Signaling Pathways -- 12.4.1 Primary ROS Sources upon Salt Stress -- 12.4.2 ROS-Dependent Initial Salt Stress Signaling Pathways -- 12.5 ROS-Mediated Low-Oxygen Sensing -- 12.5.1 Mitochondria and Plasma Membrane as ROS Sources During Hypoxia -- 12.5.2 ROS-Dependent Low-Oxygen Signaling Cascades -- 12.6 Conclusion -- Acknowledgments -- References -- 13 The Cadmium-Binding Thioredoxin O Acts as an Upstream Regulator of the Redox Plant Homeostasis -- Abstract -- 13.1 Introduction -- 13.2 Materials and Methods -- 13.2.1 Chemicals -- 13.2.2 Cloning, Expression, and Purification of Recombinant PsTrx o -- 13.2.3 Effect of Cd2+ ions on PsTrx o In Vitro -- 13.2.4 Electrochemical Measurements -- 13.2.5 Voltamperogram of Trx o: Determination of the Half-Wave Potential -- 13.2.6 Determination of Electron Mobility -- 13.2.7 Spectrum Screening -- 13.2.8 Statistical Analysis -- 13.3 Results and Discussion -- 13.3.1 In Vitro Effect of Cd2+ on Trx o Structure and Activity -- 13.3.2 Proposed Diagram for the Oxidation Mechanisms of Pea Trx o -- 13.3.3 In Vitro Effect of Cd2+ on Trx o Oxidation -- 13.3.4 Variation of the Redox Reaction of Trx o as a Function of Protein Concentration -- 13.3.5 Effect of Cd2+-Trx o Bound on the Redox Reaction -- 13.3.6 Effect of Cd2+ on the Half-Wave Potential E1/2 or Redox Potential of Trx o.
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13.3.7 Effect of Cd2+ on Electron Transfer.
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