| Inorganic and Bioinorganic Reaction Mechanisms: Application of High Pressure Techniques / R. Van Eldik ; C. Ducker-Benfer ; F. Thaler A. Roodt ; A. Abou-Hamdan ; H.P. Engelbrecht ; A.E. Merbach |
| Substitution Studies of Second and Third Row Transition Metal OXO Complexes / J.J. Cruywagen |
| Protonation, Oligomerization, and Condensation Reactions of Vanadate(V) Molybdate(V) and Tungstate(VI) / Z. Guo ; P.J. Sadler |
| Medicinal Inorganic Chemistry / R.J. Browne ; D.A. Buckingham ; C.R. Clark ; P.A. Sutton |
| The Cobalt(III)-Promoted Synthesis of Small Peptides |
| Biological and Synthetic [Fe[subscript 3]S[subscript 4]] Clusters / Michael K. Johnson ; Randall E. Duderstadt ; Evert C. Duin |
| Introduction / I.： |
| Historical Perspective / II.： |
| Occurrence and Function / III.： |
| Structures / IV.： |
| Electronic, Magnetic, and Vibrational Properties / V.： |
| Cluster Conversions / VI.： |
| Synthetic Model Compounds / VII.： |
| Mixed Metal Clusters / VIII.： |
| Future Directions / IX.： |
| References |
| The Structures of Rieske and Rieske-Type Proteins / Thomas A. Link |
| Historical Background |
| Structural Aspects |
| Spectroscopy |
| Electrochemistry |
| Biosynthesis |
| Function |
| Outlook |
| Structure, Function, and Biosynthesis of the Metallosulfur Clusters in Nitrogenases / Barry E. Smith |
| The Fe Proteins of Molybdenum Nitrogenase |
| The MoFe Proteins |
| Biosynthesis of Molybdenum Nitrogenase |
| The Mechanism of Molybdenum Nitrogenase |
| The Alternative Nitrogenases |
| Conclusions and Outlook |
| The Search for a "Prismane" Fe-S Protein / Alexander F. Arendsen ; Peter F. Lindley |
| Historical Discovery of "Prismane" Protein (Now Termed Feps) |
| Crystallographic Studies |
| Conclusion and Future Studies |
| NMR Spectra of Iron-Sulfur Proteins / Ivano Bertini ; Claudio Luchinat ; Antonio Rosato |
| Electron Relaxation Times |
| Valence Delocalization |
| Considerations on the Reduction Potential |
| Solution Structure |
| Folding |
| Perspectives |
| Nickel-Iron-Sulfur Active Sites: Hydrogenase and CO Dehydrogenase / Juan C. Fontecilla-Camps ; Stephen W. Ragsdale |
| General Concepts Regarding Nickel and Iron-Sulfur |
| Hydrogenase |
| CODH/ACS |
| Conclusions |
| FeS Centers Involved in Photosynthetic Light Reactions / Barbara Schoepp ; Myriam Brugna ; Evelyne Lebrun ; Wolfgang Nitschke |
| 2[4Fe-4S] Proteins |
| The Bridging Cluster F[subscript x] |
| [2Fe-2S] Ferredoxins |
| High-Potential Iron-Sulfur Proteins |
| The Rieske Protein |
| Evolutionary Remarks |
| Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing Bacteria / Isabel Moura ; Alice S. Pereira ; Pedro Tavares ; Jose J. G. Moura |
| Rubredoxin and Desulforedoxin |
| Desulfoferrodoxin |
| Rubrerythrin |
| Ferredoxins |
| Fuscoredoxin (Novel Fe-S Cluster) |
| APS Reductase |
| Pyruvate-Ferredoxin Oxidoreductase |
| Sulfite Reductase |
| Molybdopterin-Containing Enzymes in SRB / X.： |
| Concluding Remarks / XII.： |
| Application of EPR Spectroscopy to the Structural and Functional Study of Iron-Sulfur Proteins / Bruno Guigliarelli ; Patrick Bertrand |
| EPR Characteristics and Relaxation Properties of the Centers |
| Application of EPR to the Structural Study of Iron-Sulfur Proteins |
| Application of EPR to the Functional Study of Iron-Sulfur Centers |
| Conclusion |
| Spin-Lattice Relaxation Processes / Appendix： |
| Index |
| Contents of Previous Volumes |
| Clinical Reactivity of the Active Site of Myoglobin / Emma Lloyd Raven ; A. Grant Mauk |
| Cloning and Expression of Recombinant Myoglobin |
| Active Site Variants of Myoglobin |
| Electron Transfer Reactions of Myoglobin |
| Peroxidase Activity |
| Lipoxygenase Activity |
| Monooxygenase Activity |
| Coupled Oxidation |
| Sulfmyoglobin |
| Other Reactions of Myoglobin |
| Enzymology and Structure of Catalases / Peter Nicholls ; Ignacio Fita ; Peter C. Loewen |
| Categorization |
| Physiology |
| Kinetics |
| Structure of Type A Catalases |
| Structure of Type B Catalase-Peroxidases |
| Structure of Chloroperoxidase |
| Mechanism of the Catalytic Reaction |
| Summary |
| Horseradish Peroxidase / Nigel C. Veitch ; Andrew T. Smith |
| Biochemistry and Molecular Biology |
| General Features of the Enzyme |
| Structure and Function |
| Applications |
| Structure and Enzymology of Diheme Enzymes: Cytochrome cd[subscript 1] Nitrate and Cytochrome c Peroxidase / Vilmos Fulop ; Nicholas J. Watmough ; Stuart J. Ferguson |
| Cytochromes cd[subscript 1] |
| Diheme Cytochrome c Peroxidases |
| Binding and Transport of Iron-Porphyrins by Hemopexin / William T. Morgan ; Ann Smith |
| Biological Properties of Hemopexin |
| Biological Activities of Hemopexin |
| Physical-Chemical Properties of Hemopexin |
| Hemopexin Receptor Properties on Heme-Hemopexin |
| Structures of Gas-Generating Heme Enzymes: Nitric Oxide Synthase and Heme Oxygenase / Thomas L. Poulos ; Huiying Li ; C. S. Raman ; David J. Schuller |
| Biological Targets of NO and CO Action |
| Overview of Oxygen Activating Heme Enzymes |
| Background on NOS |
| NOS Structure |
| NOS Catalytic Structure |
| Background on HO |
| HO Structure |
| HO Catalytic Mechanism |
| The Nitric Oxide-Releasing Heme Proteins From the Saliva of the Blood-Sucking Insect Rhodnius prolixus / F. Ann Walker ; William R. Montfort |
| Spectroscopic Characterization of the Nitrophorins |
| Crystallization and Structural Determination of Nitrophorins |
| Kinetics and Thermodynamics of Ligand Binding |
| Reduction Potentials of Nitrophorins in the Absence and Presence of NO, Histamine, and Other Ligands |
| Summary and Future Directions |
| Heme Oxygenase Structure and Mechanism / Paul R. Ortiz de Montellano ; Angela Wilks |
| Biological Function of Heme Oxygenase |
| Heme Oxygenase Model Systems |
| Heme Oxygenase: The Protein |
| Human HO-1 Crystal Structure |
| Interaction with Cytochrome P450 Reductase |
| Gaseous Ligands |
| Substrate Specificity |
| The First Stage: [alpha]-meso-Hydroxylation |
| The Second Stage: [alpha]-meso-Hydroxyheme to Verdoheme |
| The Third Stage: Verdoheme to Biliverdin |
| Kinetics of the Heme Oxygenase Reaction Sequence |
| Implications of Electrophilic Heme Oxidation by an Fe[superscript III]-OOH Intermediate / XIII.： |
| Heme Degradation in Plants and Bacteria / XIV.： |
| De Novo Design and Synthesis of Heme Proteins / Brian R. Gibney ; P. Leslie Dutton |
| Natural Protein Engineering |
| De Novo Heme Proteins |
| Physical/Electrochemical Studies of de Novo Designed Heme Proteins |
| Functional Aspects |
| Diversity-based approaches to selective biomimetic oxidation catalysis / 1： |
| Selective conversion of hydrocarbons with H2O2 using biomimetic non-heme iron and manganese oxidation catalysts / 2： |
| DNA oxidation by copper and manganese complexes / 3： |
| Ligand influences in copper-dioxygen complex-formation and substrate oxidations / 4： |
| Biomimetic oxidations by dinuclear and trinuclear copper complexes / 5： |
| Green oxidation of alcohols using biomimetic Cu complexes and Cu enzymes as catalysts / 6： |
| Synergy between Theory and Experiment as Applied to H/D Exchange Activity Assays in [Fe]H2ase Active Site Models |
| Electronic Structure and Spectroscopic |
| Properties of Molybdenum and Tungsten N2, NNH, NNH2 and NNH3 |
| Complexes with Diphosphine Coligands: Insights into the End-On Terminal Reduction Pathway of Dinitrogen |
| Quantum Chemical Investigations into the Problem of Biological Nitrogen Fixation: Sellmann-Type Metal-Sulfur Model Complexes |
| Proton and Electron Transfers in [NiFe] Hydrogenase |
| Heterolytic Splitting of HH, SiH, and Other s Bonds on Electrophilic Metal Centers |
| Tetrapodal Pentadentate Nitrogen Ligands: Aspects of Complex Structure and Reactivity |
| Efficient, Ecologically Benign, Aerobic Oxidation of Alcohols |
| Visible Light Photocatalysis by a Titania Transition Metal Complex |
| Dioxygen Activation by Transition Metal Complexes |
| Atom Transfer and Free Radical Chemistry in Aqueous Media |
| Redox Reactivity of Coordinated Ligands in Pentacyano(L)ferrate Complexes |
| Carbonato Complexes: Models for Carbonic Anhydrase |
| Transition Metal Chemistry of Glucose Oxidase, Horseradish Peroxidase, and Related Enzymes |
| Properties of Transition Metal Complexes with Metal-Carbon Bonds in Aqueous Solutions as Studied by Pulse Radiolysis |
| Transition Metal Complexes with Bis(hydrazone) Ligands of 2,6-Diacetylpyridine. Hepta-Coordination of 3d Metals |
| Potential Applications for the Use of Lanthanide Complexes as Luminescent Biolabels |
| Preface |
| Tripodal Carbene and Aryloxide Ligands for Small-Molecule Activation at Electron-Rich Uranium and Transition Metal Centers / Karsten Meyer ; Suzanne C. Bart |
| Synthesis and Characterization of Ligand Precursors and Low-Valent Metal Complexes for Small-Molecule Activation / I： |
| Small-Molecule Activation / III： |
| [beta]-Cyclodextrin-Linked Ru Complexes for Oxidations and Reductions / W.-D. Woggon ; Alain Schlatter ; Hao WangIV： |
| Mimicking the Enzymatic Cleavage of Carotenoids |
| Hydrogen Transfer Reactions Catalyzed by Ruthenium Complexes Linked to [beta]-Cyclodextrin |
| Catalytic Dismutation vs. Reversible Binding of Superoxide / Ivana Ivanovic-Burmazovic |
| Catalytic Superoxide Dismutation by Seven-Coordinate Manganese and Iron Complexes as SOD Mimetics |
| Reversible Binding of Superoxide to Iron-Porphyrin Complex |
| Acknowledgment |
| Tripodal N,N,O-Ligands for Metalloenzyme Models and Organometallics / Nicolai Burzlaff |
| The '2-His-1-Carboxylate Facial Triad' in Non-Heme Iron Oxygenases |
| N,N,O-Ligands as Mimics for the '2-His-1-Carboxylate Facial Triad' |
| Structural Zinc Models |
| Homochiral Bis(pyrazol-1-yl)acetato Ligands |
| Bis(pyrazol-1-yl)acetato Ligands in Coordination Chemistry and Organometallics / V： |
| 3,3-Bis(1-methylimidazol-2-yl)propionic Acid as N,N,O-Ligand / VI： |
| Immobilization of N,N,O Complexes / VII： |
| Acknowledgements / VIII： |
| Hydroxypyranones, Hydroxypyridinones, and their Complexes / John Burgess ; Maria Rangel |
| Ligands and Complexes - Synthesis and Structure |
| Solution Properties |
| Uses and Applications |
| Nomenclature and Abbreviations |
| Late Transition Metal-Oxo Compounds and Open-Framework Materials that Catalyze Aerobic Oxidations / Rui Cao ; Jong Woo Han ; Travis M. Anderson ; Daniel A. Hillesheim ; Kenneth I. Hardcastle ; Elena Slonkina ; Britt Hedman ; Keith O. Hodgson ; Martin L. Kirk|cDjamaladdin G. Musaev ; Keiji Morokuma ; Yurii V. Geletii ; Craig L. Hill |
| Late Transition Metal-Oxo (LTMO) Complexes |
| Open-Framework Materials that Catalyze Aerobic Oxidations |
| Acknowledgments |
| Inorganic and Bioinorganic Reaction Mechanisms: Application of High Pressure Techniques / R. Van Eldik ; C. Ducker-Benfer ; F. Thaler A. Roodt ; A. Abou-Hamdan ; H.P. Engelbrecht ; A.E. Merbach |
| Substitution Studies of Second and Third Row Transition Metal OXO Complexes / J.J. Cruywagen |
| Protonation, Oligomerization, and Condensation Reactions of Vanadate(V) Molybdate(V) and Tungstate(VI) / Z. Guo ; P.J. Sadler |
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