Title:
Metalloenzymes involving amino acid-residue and related radicals
Series:
Metal ions in biological systems; 30
Publication Information:
New York : Marcel Dekker, 1994
ISBN:
9780824790936
Available:*
Library | Item Barcode | Call Number | Material Type | Item Category 1 | Status |
---|---|---|---|---|---|
Searching... | 30000003717323 | QP532 M47 1995 | Open Access Book | Book | Searching... |
On Order
Summary
Summary
This volume is devoted solely to the research area of metalloenzymes involving amino acid-residue and related radicals. Topics covered include: general considerations; structure, function and engineering of peroxidases; and ribonucleotide reductase in mammalian systems.
Table of Contents
Preface to the Series | p. iii |
Preface to Volume 30 | p. v |
Contributors | p. xiii |
Contents of Previous Volumes | p. xv |
Handbook on Toxicity of Inorganic Compounds | p. xxxii |
Handbook on Metals in Clinical and Analytical Chemistry | p. xxxiii |
Chapter 1 Free Radicals and Metalloenzymes: General Considerations | p. 1 |
1. Introduction: A Survey of Biologically Relevant Free Radicals | p. 2 |
2. Necessity of Free Radicals and Metal Ions | p. 4 |
3. Reactivities of Free Radicals | p. 7 |
4. Summary of Free Radical-Dependent Metalloenzymes | p. 11 |
Abbreviations | p. 21 |
References | p. 22 |
Chapter 2 Peroxidases: Structure, Function, and Engineering | p. 25 |
1. Introduction | p. 26 |
2. Peroxidase Crystal Structures | p. 30 |
3. Peroxidase Catalytic Mechanisms | p. 48 |
4. Peroxidase Engineering | p. 56 |
5. Conclusions | p. 65 |
Abbreviations | p. 66 |
References | p. 67 |
Chapter 3 Photosystem II | p. 77 |
1. Introduction | p. 78 |
2. Identification and Spectroscopic Studies of the Tyrosine Radicals | p. 83 |
3. Electron Transfer Reactions of the Tyrosine Radicals--Both O[subscript 2]-Evolving and Inhibited Photosystem II | p. 89 |
4. Other Radicals in Photosystem II | p. 95 |
5. Concluding Remarks | p. 99 |
Abbreviations | p. 100 |
References | p. 100 |
Chapter 4 Ribonucleotide Reductase in Mammalian Systems | p. 109 |
1. Introduction | p. 110 |
2. Mammalian Ribonucleotide Reductase | p. 110 |
3. Herpes Simplex Virus Ribonucleotide Reductase | p. 115 |
4. Comparison of Amino Acid Sequences and Spectroscopic Properties for Different Species | p. 116 |
5. Formation, Properties, and Stability of the Fe-Tyrosyl Radical Center | p. 120 |
6. Inhibitors; Radical Scavengers; Iron Chelators; Specific Peptides | p. 121 |
7. Subunit Interaction and Electron Transfer | p. 124 |
Abbreviations | p. 125 |
References | p. 125 |
Chapter 5 Manganese-Dependent Ribonucleotide Reduction and Overproduction of Nucleotides in Coryneform Bacteria | p. 131 |
1. Introduction: The Diversity of Ribonucleotide Reductase Systems | p. 132 |
2. Effects of Manganese Depletion in Coryneform Bacteria | p. 136 |
3. The Manganese-Containing Ribonucleotide Reductase of Brevibacterium ammoniagenes | p. 142 |
4. Distribution of Manganese Ribonucleotide Reductases | p. 153 |
5. Concluding Remarks--Ribonucleotide Reduction: Universal but Not Uniform | p. 156 |
Abbreviations | p. 158 |
References | p. 158 |
Chapter 6 Prostaglandin Endoperoxide Synthases | p. 163 |
1. Introduction | p. 164 |
2. PGH Synthase Isozymes | p. 167 |
3. Cyclooxygenase Catalysis | p. 171 |
4. Peroxidase Catalysis | p. 179 |
5. Cyclooxygenase-Peroxidase Interrelationships | p. 184 |
6. PGH Synthase Structure | p. 186 |
Abbreviations | p. 192 |
References | p. 192 |
Chapter 7 Diol Dehydrase from Clostridium Glycolicum: The Non-B[subscript 12]-Dependent Enzyme | p. 201 |
1. Introduction | p. 202 |
2. Diol Metabolism in C. glycolicum | p. 203 |
3. Properties of Membrane bound Diol Dehydrase from C. glycolicum | p. 206 |
4. Characterization of Diol Dehydrase | p. 209 |
5. Conclusions | p. 213 |
Abbreviations | p. 214 |
References | p. 214 |
Chapter 8 Diol Dehydrase and Glycerol Dehydrase, Coenzyme B[subscript 12]-Dependent Isozymes | p. 217 |
1. Introduction | p. 218 |
2. Purification, Properties, and Structures | p. 219 |
3. Catalytic Properties and Mechanism of Action | p. 223 |
4. Formation of Free Radicals | p. 232 |
5. Inactivation and Reactivation | p. 240 |
6. Physiological Roles | p. 244 |
7. Concluding Remarks | p. 247 |
Abbreviations | p. 248 |
References | p. 249 |
Chapter 9 Adenosylcobalamin (Vitamin B[subscript 12] Coenzyme)-Dependent Enzymes | p. 255 |
1. Survey of Adenosylcobalamin-Dependent Enzymes | p. 256 |
2. Mechanisms of the Co-C Bond Cleavage | p. 259 |
3. Mechanisms of the Subsequent Reactions | p. 269 |
4. Conclusion | p. 275 |
Abbreviations | p. 275 |
References | p. 276 |
Chapter 10 S-Adenosylmethionine-Dependent Radical Formation in Anaerobic Systems | p. 279 |
1. Introduction | p. 280 |
2. Pyruvate Formate Lyase-Activating Enzyme | p. 280 |
3. Lysine 2,3-Aminomutase | p. 300 |
4. Anaerobic Ribonucleotide Reductase | p. 306 |
5. Concluding Remarks | p. 308 |
Abbreviations | p. 309 |
References | p. 309 |
Chapter 11 The Free Radical-Coupled Copper Active Site of Galactose Oxidase | p. 315 |
1. Introduction | p. 316 |
2. Historical Survey | p. 318 |
3. Recent Developments | p. 322 |
4. Model Reactions and the Role of the Radical in Catalysis | p. 352 |
Abbreviations and Definitions | p. 356 |
References | p. 356 |
Chapter 12 Amine Oxidases | p. 361 |
1. Introduction | p. 362 |
2. Structural Properties of Amine Oxidases | p. 365 |
3. Catalytic Mechanism of Amine Oxidases | p. 380 |
4. Biological Roles of Amine Oxidases | p. 392 |
5. Conclusions and Prospects | p. 395 |
Abbreviations | p. 396 |
References | p. 397 |
Chapter 13 Bacterial Transport of and Resistance to Copper | p. 405 |
1. Introduction | p. 406 |
2. Copper in Bacterial Nutrition | p. 407 |
3. Copper Transport and Uptake | p. 409 |
4. Bacterial Systems Conferring Resistance to Excess Copper | p. 415 |
5. Concluding Remarks | p. 428 |
Definitions and Abbreviations | p. 429 |
References | p. 430 |
Author Index | p. 435 |
Subject Index | p. 469 |