| Preface to the Series | p. iii |
| Preface to Volume 38 | p. v |
| Contributors | p. xiii |
| Contents of Previous Volumes | p. xvii |
| Handbook on Toxicity of Inorganic Compounds | p. xlvii |
| Handbook on Metals in Clinical and Analytical Chemistry | p. xlviii |
| Handbook on Metalloproteins | p. xlviii |
| Peptide Bond Characteristics | p. 1 |
| Background | p. 2 |
| Proton Binding and Loss | p. 2 |
| Metal Ion Binding at the Peptide Bond | p. 3 |
| Free Energies of Peptide Bond Hydrolysis and Formation | p. 7 |
| Equilibrium Constants for Peptide Bond Formation in the Presence of Metal Ions | p. 12 |
| Peptide Oxygen Basicity Determined by Amide Amino Group Basicity | p. 16 |
| Metal Ion Effects on Rates of Peptide Bond Hydrolysis | p. 19 |
| References | p. 21 |
| Lanthanide Ion-Mediated Peptide Hydrolysis | p. 25 |
| Introduction | p. 26 |
| Amide Hydrolysis by Lanthanide Ions | p. 27 |
| Mechanism of Ce(IV) Catalysis | p. 31 |
| Cyclodextrin Complexes of Lanthanide Ions for Homogeneous Hydrolysis of Amides | p. 35 |
| Relevance of the Lanthanide-Mediated Amide Hydrolysis to DNA Hydrolysis | p. 37 |
| Conclusion | p. 38 |
| Acknowledgment | p. 39 |
| Abbreviations | p. 39 |
| References | p. 39 |
| Co(III)-Promoted Hydrolysis of Amides and Small Peptides | p. 43 |
| Introduction | p. 44 |
| Early Studies and Scope | p. 47 |
| Co(III) Linkage Isomers and Isomerization | p. 58 |
| Hydrolysis by Direct Polarization | p. 63 |
| Bimolecular Reactions of Co-OH[subscript 2]/OH | p. 72 |
| Intramolecular Reactions of CoOH[subscript 2]/OH | p. 75 |
| Kinetic Parameters and Reaction Mechanism | p. 87 |
| Related Nonmetal Hydrolysis Reactions | p. 95 |
| Abbreviations | p. 97 |
| References | p. 98 |
| Synthetic Cu(II) and Ni(II) Peptidases | p. 103 |
| Introduction | p. 104 |
| Hydrolysis of Simple Peptides by Cu(II) and Ni(II) Ions in Solution | p. 105 |
| Cleavage of Substrates Containing a Metal Binding Site by Cu(II) and Ni(II) Ions | p. 109 |
| Cleavage of Amides, Peptides, and Proteins by Defined Metal Complexes | p. 121 |
| Conclusions | p. 140 |
| Abbreviations | p. 140 |
| References | p. 141 |
| Palladium(II) and Platinum(II) Complexes as Synthetic Peptidases | p. 145 |
| Introduction | p. 146 |
| Selective Binding of Metal Complexes to Peptides and Peptide Cleavage | p. 152 |
| Cleavage of Proteins | p. 176 |
| Prospects | p. 181 |
| Acknowledgments | p. 183 |
| Abbreviations and Symbols | p. 183 |
| References | p. 184 |
| Protease Activity of 1,10-Phenanthroline-Copper Systems | p. 187 |
| Introduction | p. 188 |
| Can Free Copper(II) Ions Degrade Proteins? | p. 188 |
| Protein Degradation by the 1,10-Phenanthroline-Copper(II) Complex | p. 190 |
| Protease Activity of the Chemically Modified 1,10-Phenanthroline-Copper(II) Complex | p. 194 |
| Conclusion | p. 195 |
| Abbreviations | p. 195 |
| References | p. 196 |
| Specific Protein Degradation by Copper(II) Ions | p. 197 |
| Introduction | p. 198 |
| Peptide Sequence Specificity for Cleavage by Copper(II) Ions | p. 199 |
| Conditions Affecting the Rate of Cleavage of Peptides by Copper(II) Ions | p. 204 |
| Possible Mechanisms of Copper(II)-Mediated Hydrolysis of Peptide Bonds | p. 206 |
| Physiological Relevance of the Degradation of Proteins by Copper(II) Ions | p. 210 |
| Abbreviations | p. 210 |
| References | p. 211 |
| Artificial Iron-Dependent Proteases | p. 213 |
| Introduction: Historical Background and Concepts | p. 214 |
| Principles and Practical Aspects | p. 216 |
| Methodology | p. 226 |
| Transcription Complexes in Escherichia coli | p. 234 |
| Conclusions | p. 247 |
| Acknowledgments | p. 248 |
| Abbreviations | p. 248 |
| References | p. 249 |
| Hydroxyl Radical Footprinting of Proteins Using Metal Ion Complexes | p. 255 |
| Introduction | p. 256 |
| Experimental Methodology of Protein Footprinting | p. 258 |
| Applications of Protein Footprinting Methodology | p. 266 |
| Future Directions | p. 283 |
| Abbreviations and Definitions | p. 284 |
| References | p. 285 |
| Nickel- and Cobalt-Dependent Oxidation and Cross-Linking of Proteins | p. 289 |
| Introduction | p. 290 |
| Determinants of Nickel- and Cobalt-Dependent Oxidation | p. 292 |
| Intrinsic Sensitivity of Native Proteins | p. 299 |
| Mapping Tertiary and Quaternary Structure of Proteins | p. 302 |
| Conclusions | p. 305 |
| Abbreviations | p. 305 |
| References | p. 306 |
| Effects of Metal Ions on the Oxidation and Nitrosation of Cysteine Residues in Proteins and Enzymes | p. 313 |
| Introduction | p. 314 |
| Background: Properties and Biological Roles of Cysteine Residues | p. 315 |
| Oxidation of Cysteines | p. 316 |
| Nitrosation of Cysteines | p. 331 |
| Conclusions | p. 340 |
| Acknowledgments | p. 341 |
| Abbreviations | p. 341 |
| References | p. 343 |
| Protein Cross-Linking Mediated by Metal Ion Complexes | p. 351 |
| Introduction | p. 352 |
| Small-Molecule Cross-Linking Reagents Used Free in Solution | p. 356 |
| Development of Affinity Cross-Linking Reagents: Use of Peptides or Proteins to Deliver a Cross-Linking Reagent Site-Specifically | p. 368 |
| Conclusions | p. 379 |
| Abbreviations | p. 379 |
| References | p. 380 |
| Ferrocenoyl Amino Acids and Peptides: Probing Peptide Structure | p. 385 |
| Introduction: Organometallic Probes in Biological Systems | p. 386 |
| Synthetic Studies of Ferrocenoyl Amino Acids and Peptides | p. 387 |
| Structural and Theoretical Studies | p. 390 |
| Electrochemistry of Ferrocenoyl Amino Acids and Peptides | p. 398 |
| Summary | p. 404 |
| Acknowledgment | p. 406 |
| Abbreviations | p. 406 |
| References | p. 407 |
| Synthetic Analogs of Zinc Enzymes | p. 411 |
| Introduction | p. 412 |
| Structural and Functional Models of Zinc Enzymes as Classified by Active Site Composition | p. 417 |
| Use of Metal Ion Substitution to Provide Insight into the Structures and Mechanisms of Action of Zinc Enzymes | p. 445 |
| Perspectives | p. 451 |
| Acknowledgments | p. 452 |
| Abbreviations | p. 452 |
| References | p. 453 |
| Mimicking Biological Electron Transfer and Oxygen Activation Involving Iron and Copper Proteins: A Bio(in)organic Supramolecular Approach | p. 461 |
| Introduction | p. 462 |
| Mimics for Iron-Sulfur Proteins | p. 474 |
| Mimics for Blue Copper Proteins | p. 522 |
| Cytochrome P450 Mimics | p. 534 |
| Mimics for Oxygen Binding and Activation by Copper Proteins | p. 568 |
| Concluding Remarks | p. 601 |
| Acknowledgments | p. 602 |
| Abbreviations | p. 602 |
| References | p. 604 |
| Subject Index | p. 657 |
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