Redox biochemistry:
Gespeichert in:
| Weitere Verfasser: | |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Hoboken, N.J.
Wiley-Interscience
2008
|
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | Literaturangaben |
| Beschreibung: | XX, 317 S. Ill., graph. Darst. |
| ISBN: | 9780471786245 0471786241 |
Internformat
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| 245 | 1 | 0 | |a Redox biochemistry |c ed. by Ruma Banerjee ... |
| 264 | 1 | |a Hoboken, N.J. |b Wiley-Interscience |c 2008 | |
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Datensatz im Suchindex
| _version_ | 1804142688635715584 |
|---|---|
| adam_text | — CONTENTS
Contributors xiii
List of Abbreviations xvii
Preface xix
1. Redox Metabolism and Life 1
By Ruma Banerjee
1.1. Redox Biochemistry and the Evolution of Life 1
1.2. Global Redox Cycles 4
1.3. Major Bioenergetic Cycles 6
1.3.A. Photosynthesis 6
I.3.B. Aerobic Respiration 7
2. Antioxidant Molecules and Redox Cofactors 11
Edited by Donald Becker
2.1.Glutathione 11
By Joseph J. Barycki
2.1 .A. Biological Functions 13
2.l.B. Biosynthesis 14
2.l.C. Degradation 16
2.1 .D. Other Thiol-Based Redox Buffers 21
2.2. Ascorbate 22
By Han Asard
2.2.A. Ascorbate Chemistry 22
2.2.B. Ascorbate Biosynthesis 23
2.2.C. Ascorbate Recycling 25
2.2.D. Ascorbate Transport 26
2.2.E. Importance of Ascorbate in Stress and Disease 26
2.3. Other Antioxidants 27
By Julie M. Stone and Mark A. Wilson
2.3.A. Lipid-Soluble Antioxidants . 28
vii
Viii CONTENTS
2.3.B. Water-Soluble Antioxidants 31
2.3.C. Antioxidants and Human Health 32
2.4. Redox Coenzymes 35
By Ruma Banerjee and Donald F. Becker
2.4.A. Flavin 35
2.4.B. NAD 39
2.4.C. Quinones 40
2.4.D. Pterins and Molybdopterins 42
2.4.E. Folk Acid 46
3. Antioxidant Enzymes 49
Edited by Vadim Gladyshev
3.1. ROS-Dependent Enzymes 50
By Irwin Fridovich and Leslie B. Poole
3.1.A. Catalase 50
3.I.B. Superoxide Dismutase 55
3.l.C. Peroxiredoxins 59
3.I.D. Alkyl Hydroperoxide Reductases 65
3.2. The Thioredoxin System 68
By Arne Holmgren
3.2.A. Thioredoxin 68
3.2.B. Thioredoxin Reductase 71
3.3. The Glutathione System 74
By Marjorie F. Lou
3.3.A. Glutathione Reductase 75
3.3.B. Glutaredoxin (Thioltransferase) 78
3.4. Repair Enzymes 84
By Vadim N. Gladyshev, Sheila S. David,
and By Leslie B. Poole
3.4.A. Methionine Sulfoxide Reductases 84
3.4.B. DNA Repair Enzymes 87
3.4.C. Sulfiredoxins 94
3.5. Detoxification Enzymes 97
By Robert L. Osborne, John H. Dawson,
and Shelly D. Copley
3.5.A. Cytochrome P450 Enzymes: Structure,
Function, and Mechanism 97
3.5.B. GSH Transferases 104
3.6. Oxidative Folding 113
By Hiroshi Kadokura, Jon Beckwith, and Hiram F. Gilbert
CONTENTS iX
3.6.A. Disulfide Bond Formation in Bacteria 113
3.6.B. Disulfide Bond Formation in Eukaryotes 120
3.7. Other Antioxidant Enzymes 127
By Vadim N. Gladyshev and Stephen W. Ragsdale
3.7.A. Selenoproteins 127
3.7 .B. Heme Oxygenase 131
4. Redox Regulation of Physiological Processes 135
Edited by Martin Dickman
4.1. Reactive Oxygen, Nitrogen, and Thiol-Based Signal
Transduction 136
By lisa I. Rovira and Toren Finkel
4.1 .A. Nitric Oxide Signaling 136
4.I.B. Carbon Monoxide Signaling 141
4.l.C. Superoxide and Hydrogen Peroxide 143
4.1 .D. Other Novel Redox Molecules 147
4.2. Role of Nitric Oxide Synthases in Redox Signaling 148
By Bettie Sue Masters
4.2.A. Characterization of the Nitric Oxide Synthases 149
4.2.B. Regulation of Nitric Oxide Synthases by Intrinsic
Elements 150
4.2.C. Extrinsic Regulation of Nitric Oxide Synthases 152
4.2.D. Interactions of NO with Other Proteins and Enzymes 152
4.3. Redox Regulation of Genes 154
By Martin B. Dickman
4.3.A. MAP Kinase/Cell Cycle 154
4.3.B. Redox Control of Gene Expression 155
4.3.C. Peptide Editing and Thiol-Mediated Redox Regulation 156
4.4. Redox Regulation of Apoptosis 158
By Martin B. Dickman
4.4.A. Apoptotic Pathways 158
4.4.B. Reactive Oxygen Species and Apoptosis 159
4.5. Metal Homeostasis 162
By Jaekwon Lee
4.5.A. Physiological Significance of Metal Metabolism 163
4.5.B. Metal Uptake from the Extracellular Environment 164
4.5.C. Intracellular Metal Distribution by Target-Specific
Chaperones 165
4.5.D. Subcellular Membrane Metal Transporters 167
X CONTENTS
4.5.E. Heme and Iron-Sulfur Cluster Synthesis 168
4.5.F. Cellular Storage 168
4.5.G. Metal Export 168
4.5.H. Regulation of Metal Metabolism 169
4.5.1. Genetic Disorders in Metal Metabolism 171
4.5.J. Perturbation of Metal Homeostasis and Degenerative
Disorders 172
4.6. Redox Enzymology 173
By Stephen W. Ragsdale
4.7. Circadian Clock and Heme Biosynthesis 177
By Cheng Chi Lee
A.I.A. Cyclic Expression of Heme Binding Proteins 177
4.7.B. Circadian Clock Mechanism 178
4.7.C. PAS Is a Heme Binding Domain 179
4.7.D. Expression of Npas2 Is Controlled by mPER2 180
4.7.E. NPAS2 Regulates Expression of Aminolevulinate
Synthase 1 180
5. Pathological Processes Related to Redox 183
Edited by Ruma Banerjee
5.1. Protein Modification 184
By Earl R. Stadtman
5.1 .A. Protein Oxidation and Aging 184
5.1 .B. Mechanisms of Protein Oxidation 184
5.1 .C. Peptide Bond Cleavage 187
5.1 .D. Oxidation of Amino Acid Residue Side Chains 188
5.1 .E. Beta Scission of Amino Acid Side Chains 189
5.1 .F. Generation of Protein Carbonyl Derivatives 189
5.1 .G. Formation of Protein Cross-Linked Derivatives 193
5.I.H. Role of Protein Oxidation in Aging 193
5.2. Oxidative Stress in the Eye: Age-Related Cataract and Retinal
Degeneration 194
By Marjorie E Lou and John W. Crabb
5.2.A. Oxidative Stress and Cataract 195
5.2.B. Oxidative Stress and Retinal Pathology 199
5.3. Redox Mechanisms in Cardiovascular Disease: Chronic Heart
Failure 204
By George J. Rozanski
5.3.A. Excitation-Contraction Coupling in Cardiac Myocytes 204
5.3.B. Role of Oxidative Stress in Chronic Heart Failure 206
CONTENTS Xi
5.3.C. Redox Modulation of Ca2+ Handling Proteins 206
5.3.D. Hypertrophy and Cell Death 209
5.3.E. Extracellular Matrix Remodeling 209
5.4. Role of Reactive Oxygen Species in Carcinogenesis 212
By Suresh Veeramani and Ming-Fong Lin
5.4.A. ROS Act as Growth Signaling Messengers 212
5.4.B. Phosphatases Are Prime Targets for ROS During Growth
Stimulation 212
5.4.C. Uncontrolled Production of ROS is Carcinogenic 214
5.4.D. ROS Can Induce Carcinogenic DNA and Protein
Adducts 215
5.4.E. ROS Can Affect DNA Methylation and Gene
Expression 216
5.4.F. Mitochondrial DNA Mutations Are Induced by
ROS 216
5.4.G. Clinical Trials on Antioxidant Supplementation Against
Cancer 216
5.5. Oxidative Stress and the Host-Pathogen Interaction 218
By Greg A. Somerville
5.5.A. Neutrophils and the Innate Immune Response 219
5.5.B. Bacterial Targets of Oxidative Damage 220
5.5.C. Regulating the Oxidative Stress Response 221
5.5.D. The Oxidative Stress Response 223
5.5.E. Evasion of the Innate Immune Response 223
6. Specialized Methods 227
Edited by Stephen Ragsdale
6.1. Mass Spectrometry Applications for Redox Biology 228
By Ashraf Raza and John R. Engen
6.1 .A. Mass Spectrometer 228
6.1 .B. Applications of Mass Spectrometry 231
6.l.C. Hydrogen Exchange Mass Spectrometry 236
6.2. Electron Paramagnetic Resonance (EPR) for the Redox
Biochemist 237
By Stephen W. Ragsdale and Javier Seravalli
6.2.A. Introduction to Magnetic Resonance Spectroscopy 237
6.2.B. Basic EPR Theory 239
6.2.C. Appearance of the EPR Spectrum 240
6.2.D. The EPR Experiment 240
Xii CONTENTS
6.2.E. The Conventional EPR Spectrometer: Detection of the
Signal 241
6.2.F. Sensitivity and Saturation in EPR 244
6.2.G. Measuring the Concentration of Spins 244
6.2.H. Nuclear Hyperfine and Spin-Spin Interactions 246
6.3. Redox Potentiometry 247
By Donald F. Becker
6.3.A. Midpoint Potential 247
6.3.B. Redox-Linked Processes 248
6.3.C. Potentiometric Technique 249
6.4. Bioinformatics Methods to Study Thiol-Based Oxidoreductases 251
By Dmitri E. Fomenko and Vadim N. Gladyshev
6.4.A. Identification of Redox-Active Cysteines in Proteins 251
6.4.B. Cysteine-Based Redox Motifs 253
6.4.C. Conserved Cysteines in Metal-Binding Proteins 253
6.4.D. Secondary Structure Context of Redox-Active Cysteines 253
6.4.E. Structure Modeling 255
6.4.F. Comparative Sequence Analysis of Thiol-Based
Oxidoreductases 255
6.5. Electrophysiology 256
By Mark P. Thomas and Harold D. Schultz
6.5.A. Electrophysiology Part I: Ion Channel Physiology 256
6.5.B. Electrophysiology Part II 263
6.6. Methods to Detect Reactive Metabolites of Oxygen and Nitrogen 272
By Matthew B. Grisham
6.6.A. Detection of the Superoxide Anion Radical 273
6.6.B. Detection of Hydrogen Peroxide 274
6.6.C. F2-Isoprostanes as Indicators of Lipid Peroxidation
In Vivo 276
6.6.D. Measurement of the GSSG/GSH Redox Couple in Cells
and Tissue 277
6.6.E. Methods to Detect NO and Its Oxidized Metabolites
In Vitro and In Vivo 277
6.6.F. Detection of 5-Nitrosothiols by Colorimetric and
Fluorimetric Methods 281
6.6.G. Is the Presence of 3-Nitrotyrosine a Specific Footprint for
Peroxynitrite? 283
Index 285
|
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| indexdate | 2024-07-09T22:35:45Z |
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| spelling | Redox biochemistry ed. by Ruma Banerjee ... Hoboken, N.J. Wiley-Interscience 2008 XX, 317 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Literaturangaben Physiologische Chemie (DE-588)4076124-1 gnd rswk-swf Antioxidans (DE-588)4142729-4 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Physiologische Chemie (DE-588)4076124-1 s Antioxidans (DE-588)4142729-4 s DE-604 Banerjee, Ruma edt HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=020123199&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Redox biochemistry Physiologische Chemie (DE-588)4076124-1 gnd Antioxidans (DE-588)4142729-4 gnd |
| subject_GND | (DE-588)4076124-1 (DE-588)4142729-4 (DE-588)4143413-4 |
| title | Redox biochemistry |
| title_auth | Redox biochemistry |
| title_exact_search | Redox biochemistry |
| title_full | Redox biochemistry ed. by Ruma Banerjee ... |
| title_fullStr | Redox biochemistry ed. by Ruma Banerjee ... |
| title_full_unstemmed | Redox biochemistry ed. by Ruma Banerjee ... |
| title_short | Redox biochemistry |
| title_sort | redox biochemistry |
| topic | Physiologische Chemie (DE-588)4076124-1 gnd Antioxidans (DE-588)4142729-4 gnd |
| topic_facet | Physiologische Chemie Antioxidans Aufsatzsammlung |
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