The Coordination Chemistry of Metalloenzymes

I: The Coordination Properties of the Active Site of Zinc Enzymes.- 1. Introduction.- 2. The Residues Coordinated at the Zinc Ion.- 3. The Acid-Base Properties of Coordinated Water.- 4. The Electronic Spectra of Cobalt (II) Derivatives.- 5. The Water 1H NMR Studies.- 6. The Implications on the Catalytic Mechanism.- II: Coordinated Solvent Molecules in Metalloenzymes and Proteins Studied Using NMRD.- 1. Introduction.- 2. The "Fluoromet" Mechanism.- 3. Fe3+ - Transferrin.- 4. Cu2+ - and V02+ - Transferrin.- 5. Co2+ - Carbonic Anhydrase.- 6. Alcohol Dehydrogenase.- 7. Mn2+ - Carboxypeptidase A.- 8. Conclusions.- III: 113Cd Nuclear Magnetic Resonance Studies of Zinc Metalloproteins.- 1. Introduction.- 2. Chemical Shifts.- 3. Sensitivity.- 4. Information Content.- 5. Concluding Remarks.- IV: Carbonic Anhydrase: Structure, Kinetics, and Mechanism.- 1. Introduction.- 2. Structure.- 3. Kinetics.- 4. Mechanism.- V: Metal Ion Promoted Hydrolysis of Nucleoside 5'-Triphosphates.- 1. Introduction.- 2. Results and Discussion.- VI: Models of Metalloenzymes: Carboxypeptidase A.- 1. Introduction.- 2. Metal Ion Catalyzed Hydrolysis of Amides and Esters.- 3. Results and Discussion.- 4. Cu2+ Mediated Amide Hydrolysis.- 5. Conclusions.- VII: Spectroscopic Studies on Cobalt(II) Carboxypeptidase A.- VIII: Coordination Properties and Mechanistic Aspects of Liver Alcohol Dehydrogenase.- 1. Introduction.- 2. Coordination Chemistry of Metallo Alcohol Dehydrogenases.- 3. Mechanistic Aspects.- IX: Metal-Directed Affinity Labelling and Promoted Alkylation of a Thiol Liganded to the Catalytic Metal Ion in Liver Alcohol Dehydrogenase.- 1. Introduction.- 2. Experimental.- 3. Results and Discussion.- X: Ligand Sphere Transitions: A New Concept in Zinc-Enzyme Catalysis.- 1. Introduction.- 2. Experimental Background.- 3. The Proposed Model Concept.- XI: Molecular Mechamisms of the Superoxide Dismutase Activity of the Cuprozinc Protein of Eucaryotic Cells (CuZn Superoxide Dismutase).- 1. Molecular Properties of the Protein.- 2. General Mechanism of the Superoxide Dismutation by the Copper of the Protein.- 3. Inactivation of the Enzyme.- 4. Inhibition of the Enzyme.- 5. Role of the Zinc.- XII: A Comment on Anion Binding to Superoxide Dismutase.- XIII: Kinetic and Magnetic Resonance Studies on Amine Oxidases.- 1. Introduction.- 2. Studies on the Copper Cofactor.- 3. Mechanistic Studies.- XIV: Metal Coordination and Mechanism of Blue Copper Containing Oxidases.- 1. Introduction.- 2. Chemical Composition and Reactions Catalyzed.- 3. Spectroscopic Data.- 4. Oxidation-Reduction Properties.- 5. The Catalytic Mechanism.- XV: Metal Replacement Studies of Chinese Laccase.- 1. Introduction.- 2. Metal-Replacement Studies of Small Blue Proteins.- 3. The Removal and Replacement of Copper from Chinese Laccase.- 4. The Preparation of a Mixed-Metal Hybrid of Laccase.- XVI: Reactions of Rhus Vernicifera Laccase with Azide and Fluoride, Formation of a "Half-Met-N3 -Type" Binding.- 1. Reactions with N3- as Studied by EPR.- 2. Reactions with N3- in the Presence of Redox Reagents.- 3. Half-Met-N3-Type Binding in Laccase.- 4. Reactions with Fluoride.- 5. Temperature Effects.- XVII: Structural Magnetic Correlations in Exchange Coupled Systems.- 1. Spin Hamiltonian Approach to Exchange Coupling.- 2. Molecular Orbital Approach to Exchange Coupling.- XVIII: Structural and Magnetic Investigations on Model CU4O4 Cubane-Like Clusters.- 1. Introduction.- 2. Structural Description.- 3. Magnetic Properties and Structural Data.- 4. Extension of the Correlations Between Magnetism and Structures.- 5. Example.- XIX: Neurospora Tyrosinase: Intrinsic and Extrinsic Fluorescence.- 1. Introduction.- 2. Intrinsic Fluorescence.- 3. Extrinsic Fluorescence.- XX: Comparison of Two Fungal Tyrosinases.- 1. Introduction.- 2. Molecular Properties.- 3. Properties of the Copper Site.- 4. Identification of Endogenous Ligands.- 5. Inhibition by Anions.- XXI: Activation of Molecular Oxygen.- 1. Introduction.- 2. Autoxidation Reactions.- 3. Wacker Oxidations.- 4. Oxidations by Metal Bound 02.- 5. Oxidations by Products Derived from Metal-O2 Species.- 6. Oxygen Atom Transfer Reactions.- 7. Conclusion.- XXII: Mossbauer Studies on Putidamonooxin - A New Type of [2Fe-2S] Containing Oxygenase Component with a Mononuclear Non-Heme Iron Ion as Cofactor.- 1. Introduction.- 2. Mossbauer Spectroscopic Investigation.- 3. Conclusion.- XXIII: The Enzyme-Substrate Interaction in the Catechol Dioxygenases.- XXIV: Ferric Nitrilotriacetate: An Active Center Analogue of Pyrocatechase.- XXV: Stereoselective Peroxidatic Activity of Iron(III) Complex Ions Supported on Polypeptides.- XXVI: NMR Studies of Cytochromes.- 1. Introduction.- 2. Class II Cytochromes c.- 3. Low Spin Cytochromes.- 4. Electron Transfer Mechanisms.- XXVII: The Structure of the Metal Centers in Cytochrome c Oxidase.- 1. Introduction.- 2. The Metal Centers.- 3. Summary.- XXVIII: Models of Metalloenzymes: Peroxidase and Cytochrome P-450.- 1. Introduction.- 2. Model Systems.- XXIX: Coordination Chemistry of Cytochrome P-450 and Herne Models.- 1. Introduction: Occurrence and Function of Cytochrome P450-Dependent Monooxygenases.- 2. The Catalytic Cycle of Cytochrome P450.- 3. Cytochrome P450-Iron Comlexes Formed by Direct Interaction with Organic Compounds.- 4. Cytochrome P450-Iron-Metabolite Complexes.- 5. Conclusion: The Unique Richness of Cytochrome P450 Coordination Chemistry.- XXX: Mossbauer Studies of Synthetic Analogues for the Active Site in Cytochromes P450.- 1. Introduction.- 2. Preparation of the Compounds.- 3. X-ray Structures.- 4. Mossbauer Studies.- 5. Molecular Orbital Calculations and ?EQ- Interpretation.- XXXI: Magnetic Circular Dichroism Spectroscopy as a Probe of Ferric Cytochrome P-450 and its Ligand Complexes.- 1. Introduction.- 2. Materials and Methods.- 3. Results and Discussion.- 4. Conclusion.