| Preface to the Series |
| Preface to Volume 38 |
| Contributors |
| Contents of Previous Volumes |
| Handbook on Toxicity of Inorganic Compounds |
| Handbook on Metals in Clinical and Analytical Chemistry |
| Handbook on Metalloproteins |
| Peptide Bond Characteristics / R. Bruce MartinChapter 1： |
| Background / 1.： |
| Proton Binding and Loss / 2.： |
| Metal Ion Binding at the Peptide Bond / 3.： |
| Free Energies of Peptide Bond Hydrolysis and Formation / 4.： |
| Equilibrium Constants for Peptide Bond Formation in the Presence of Metal Ions / 5.： |
| Peptide Oxygen Basicity Determined by Amide Amino Group Basicity / 6.： |
| Metal Ion Effects on Rates of Peptide Bond Hydrolysis / 7.： |
| References |
| Lanthanide Ion-Mediated Peptide Hydrolysis / Makoto KomiyamaChapter 2： |
| Introduction |
| Amide Hydrolysis by Lanthanide Ions |
| Mechanism of Ce(IV) Catalysis |
| Cyclodextrin Complexes of Lanthanide Ions for Homogeneous Hydrolysis of Amides |
| Relevance of the Lanthanide-Mediated Amide Hydrolysis to DNA Hydrolysis |
| Conclusion |
| Acknowledgment |
| Abbreviations |
| Co(III)-Promoted Hydrolysis of Amides and Small Peptides / David A. Buckingham ; Charles R. ClarkChapter 3： |
| Early Studies and Scope |
| Co(III) Linkage Isomers and Isomerization |
| Hydrolysis by Direct Polarization |
| Bimolecular Reactions of Co-OH[subscript 2]/OH |
| Intramolecular Reactions of CoOH[subscript 2]/OH |
| Kinetic Parameters and Reaction Mechanism |
| Related Nonmetal Hydrolysis Reactions / 8.： |
| Synthetic Cu(II) and Ni(II) Peptidases / Gregory M. Polzin ; Judith N. BurstynChapter 4： |
| Hydrolysis of Simple Peptides by Cu(II) and Ni(II) Ions in Solution |
| Cleavage of Substrates Containing a Metal Binding Site by Cu(II) and Ni(II) Ions |
| Cleavage of Amides, Peptides, and Proteins by Defined Metal Complexes |
| Conclusions |
| Palladium(II) and Platinum(II) Complexes as Synthetic Peptidases / Nebojsa M. Milovic ; Nenad M. KosticChapter 5： |
| Selective Binding of Metal Complexes to Peptides and Peptide Cleavage |
| Cleavage of Proteins |
| Prospects |
| Acknowledgments |
| Abbreviations and Symbols |
| Protease Activity of 1,10-Phenanthroline-Copper Systems / Makoto Kito ; Reiko UradeChapter 6： |
| Can Free Copper(II) Ions Degrade Proteins? |
| Protein Degradation by the 1,10-Phenanthroline-Copper(II) Complex |
| Protease Activity of the Chemically Modified 1,10-Phenanthroline-Copper(II) Complex |
| Specific Protein Degradation by Copper(II) Ions / Geoffrey AllenChapter 7： |
| Peptide Sequence Specificity for Cleavage by Copper(II) Ions |
| Conditions Affecting the Rate of Cleavage of Peptides by Copper(II) Ions |
| Possible Mechanisms of Copper(II)-Mediated Hydrolysis of Peptide Bonds |
| Physiological Relevance of the Degradation of Proteins by Copper(II) Ions |
| Artificial Iron-Dependent Proteases / Saul A. Datwyler ; Claude F. MearesChapter 8： |
| Introduction: Historical Background and Concepts |
| Principles and Practical Aspects |
| Methodology |
| Transcription Complexes in Escherichia coli |
| Hydroxyl Radical Footprinting of Proteins Using Metal Ion Complexes / Tomasz Heyduk ; Noel Baichoo ; Ewa HeydukChapter 9： |
| Experimental Methodology of Protein Footprinting |
| Applications of Protein Footprinting Methodology |
| Future Directions |
| Abbreviations and Definitions |
| Nickel- and Cobalt-Dependent Oxidation and Cross-Linking of Proteins / Steven E. Rokita ; Cynthia J. BurrowsChapter 10： |
| Determinants of Nickel- and Cobalt-Dependent Oxidation |
| Intrinsic Sensitivity of Native Proteins |
| Mapping Tertiary and Quaternary Structure of Proteins |
| Effects of Metal Ions on the Oxidation and Nitrosation of Cysteine Residues in Proteins and Enzymes / Ann M. English ; Dean E. WilcoxChapter 11： |
| Background: Properties and Biological Roles of Cysteine Residues |
| Oxidation of Cysteines |
| Nitrosation of Cysteines |
| Protein Cross-Linking Mediated by Metal Ion Complexes / Kathlynn C. Brown ; Thomas KodadekChapter 12： |
| Small-Molecule Cross-Linking Reagents Used Free in Solution |
| Development of Affinity Cross-Linking Reagents: Use of Peptides or Proteins to Deliver a Cross-Linking Reagent Site-Specifically |
| Ferrocenoyl Amino Acids and Peptides: Probing Peptide Structure / Heinz-Bernhard Kraatz ; Marek GalkaChapter 13： |
| Introduction: Organometallic Probes in Biological Systems |
| Synthetic Studies of Ferrocenoyl Amino Acids and Peptides |
| Structural and Theoretical Studies |
| Electrochemistry of Ferrocenoyl Amino Acids and Peptides |
| Summary |
| Synthetic Analogs of Zinc Enzymes / Gerard ParkinChapter 14： |
| Structural and Functional Models of Zinc Enzymes as Classified by Active Site Composition |
| Use of Metal Ion Substitution to Provide Insight into the Structures and Mechanisms of Action of Zinc Enzymes |
| Perspectives |
| Mimicking Biological Electron Transfer and Oxygen Activation Involving Iron and Copper Proteins: A Bio(in)organic Supramolecular Approach / Martinus C. FeitersChapter 15： |
| Mimics for Iron-Sulfur Proteins |
| Mimics for Blue Copper Proteins |
| Cytochrome P450 Mimics |
| Mimics for Oxygen Binding and Activation by Copper Proteins |
| Concluding Remarks |
| Subject Index |
| Preface to the Series |
| Preface to Volume 38 |
| Contributors |
| Contents of Previous Volumes |
| Handbook on Toxicity of Inorganic Compounds |
| Handbook on Metals in Clinical and Analytical Chemistry |
