Chemistry of Metalloproteins: Problems and Solutions in Bioinorganic Chemistry -- Contents -- Preface -- 1 Introduction -- Proteins: Formation, Structures, and Metalloproteins -- Organelles and Their Functions -- Structure of DNA -- Cell Growth and Division -- Protein Synthesis -- Common Natural α-Amino Acids -- Peptide Chain Formation -- Protein physiological functions -- Structural Features of Proteins -- Causes of Polypeptide Chain Folding -- Metal Amino Acid Complexes -- Comparison of P-O versus M-O Bond Scission Rates for Row 3 Elements -- Redox Advantages: Sulfur versus Phosphorus -- Bioenergetic Phosphate Derivatives -- References -- 2 Alkali and Alkaline Earth Cations -- References -- 3 Nonredox Metalloenzymes -- Carboxypeptidases -- What are the main functions of carboxypeptidases? -- What are the main types of carboxypeptidases? -- What are the requirements to stimulate carboxypeptidase-A and carboxypeptidase-B? -- What are the main structural features of carboxypeptidase-A and carboxypeptidase-B? -- How can Zn2+ be extracted from carboxypeptidase-A and carboxypeptidase-B? What are the consequences of metal ion removal? -- What are the spectral consequences when Zn2+ is replaced by Co2+ in carboxypeptidases? -- Describe the role of Zn2+ in carboxypeptidase-A and carboxypeptidase-B. -- Design models to mimic the role of the metal ion in carboxypeptidase-A and carboxypeptidase-B. -- Carbonic Anhydrase -- What are the main functions of carbonic anhydrase? -- Conversion of carbonic acid to CO2 and H2O is a spontaneous process. Why is carbonic anhydrase needed? -- What are the main structural and chemical features of carbonic anhydrase? -- Describe the role of the metal ion in carbonic anhydrase. -- What are the possible mechanisms that describe the action of carbonic anhydrase?.

Design models for the carbonic anhydrase, and what do they reveal? -- Rate Constants -- Alcohol Dehydrogenase -- What is the catalytic role and the structural features of the alcohol dehydrogenases? -- What is the sequence of events during the reaction of alcohol dehydrogenase? -- A number of model systems have been investigated to study the influence of Zn2+ on the reactivity of the carbonyl -- give an example. -- References -- 4 Copper Proteins -- Introduction -- Electronic Spectra of Copper Ions -- What are the structural and spectral features of copper(II)-peptide complexes in the visible region? -- ESR Spectra of Copper Ions -- How can ESR spectra be used as a ``spectral probe ́́to study copper enzymes? -- Define -- How do the nuclear-spin of Cu2+ ion and the attached ligands affect the ESR signal? How can the hyperfine and superhyperfine splitting be used as a ``spectral probe ́́for studying the copper enzymes? -- How may the spectrochemical series and the stereochemistry affect g-values of Cu2+ ion and what is the significance of All-gll trend? -- Copper Proteins -- Identify the significant roles of copper in the biological process, classify, give examples, and explain their functions and main chemical properties. -- Plastocyanin -- Identify the biological function of plastocyanin and the role of the cooper ion. -- Find the concentration of Cu+ ion in an aqueous solution at 298 K. Then, identify the role of the polypeptide chain in the biological function of plastocyanin. -- What are the upper and lower limits of redox potential of the biological systems at pH 7? -- Arrange these potentials in a diagram showing possible electron pathway. -- What is the common mechanism of electron transfer for simple copper complexes and give a model example? Explain the factors that may account for the unusual rapid electron transfer in plastocyanin.

Azurin and Stellacyanin -- Show the resemblances among plastocyanin, azurin, and stellacyanin -- Design synthetic models for plastocyanin -- Superoxide Dismutase -- The direct reduction of O2 - is toxic. How do biological systems handle this product? Give an example of Cu type II proteins -- what is the significant role of the metal ion? -- What are the structural features necessary for a metal ion to have SOD activity? Propose a mechanism for the action of SOD. -- Explain the in vitro toxicity of superoxide ``O2- ́́-- What are the structural features of superoxide dismutase? -- Hemocyanin -- Biological Function of Hemocyanin and Role of Copper Ion -- Ascorbic Oxidase -- What is the biological role of the ascorbic acid oxidase and the significance of copper in ascorbate oxidase? Give a biomimetic model. -- References -- 5 Iron Proteins -- Introduction -- Electronic Spectra of Iron Ions -- Discuss the possible electronic ground states and the allowed electronic transitions bands of iron (II) and iron (III) complexes. -- Mössbauer Spectroscopy of Iron Ions -- Nuclear Resonance Absorption -- Basic Principles -- Quadruple Splitting -- Isomer Shift -- ESR Spectra of Iron (III) -- ESR and Magnetic Susceptibility -- g-Values of Ferric Ion -- Iron Bioavailability -- Iron: Most Abundant Transition Metal in Biological Systems -- Siderophores -- Role and Chemical Features -- Classes and Examples -- Synthetic Siderophores -- Iron Storage and Transfer Proteins -- Iron Storage Proteins -- Ferritin -- Binding and Release of Iron Ions -- Transferrin -- Iron Transport Proteins -- Conditional Binding and Structural Analysis -- Mechanism for Iron Delivery -- Spectral and Structural Analysis -- Dioxygenase Iron Proteins -- Reactions of Oxygen Molecules -- Organic Compounds and Oxygen Molecule -- Oxygen Fixation -- Products of Enzymatic Oxygen Insertion.

Structural and Chemical Characterization of Active Site -- Reaction Mechanism -- Intradiol Versus Extradiol Mechanism -- Oxygenase Mimics -- Iron-Sulfur Proteins -- Classification -- Rubredoxin -- Roles, Sources, and Characterization -- Structural and Ligation Features of Rubredoxin -- Metal Removal -- Model compounds -- Ferredoxins -- Roles and Types -- 2Fe-2S Ferredoxins -- Sources and Chemical Characteristics -- Iron Ions and Active Center -- Sulfur Ligation -- Valence-Trapped Dimers -- Exchange Coupling Constant, J, in Antiferromagnetic and Ferromagnetic couplings -- 4Fe-4S Ferredoxins -- Active Site and Chemical Features -- Redox Potential -- Core Extrusion Reactions -- Active Site Analogues -- Aconitase -- Forms, Roles, and Structures -- Reaction Mechanism -- Conjugated Fe-S Proteins -- Hydroxylases -- Role, Chemical Features, and Reaction Mechanism -- Hydrogenases -- Roles and Types -- Sources, Reactions, and ESR Investigations -- Chemical Structures -- Dihydrogen and Dihydride Complexes -- Catalytic Mechanism -- Nitrogenases -- Reactions Catalyzed by Nitrogenase -- Nitrogenase and Kinetically Inert Reactions -- Structural Features -- Role of each Component in Nitrogenase -- Dinitrogen Complexes -- Catalytic Mechanism -- Binuclear Iron Proteins -- Examples and Role -- Hemerythrin -- Biological Sources -- Oxygen-Carrying Proteins -- Structural Features -- Chemical Combination Reactions -- Electronic Spectra -- Mössbauer Data and Molecular Characterization -- Ribotide Reductase, Purple Acid Phosphate, and Methane Monooxygenase -- Ribotide Reductase -- Purple Acid Phosphatase in Beef Spleen -- Methane Monooxygenase -- Chemistry of Diiron Enzymes -- Hemoproteins: Classification and Behavior of Heme in Absence of Globins -- Prosthetic Group -- Hemoproteins -- Conformations in Hemoproteins -- Diverse Functions of Heme Group -- Heme chemistry.

Myoglobin and Hemoglobin -- Biological Oxygen Carriers -- Myoglobin -- Biological Roles and Properties -- Diamagnetic Oxymyoglobin -- Ligand Binding and Myoglobin -- Hemoglobin -- Role and Properties -- Oxygen Binding -- Statistic Analysis and Difficulties -- Bohr Effect -- Oxygenation and Structural Alternations -- Monod-Wyman-Changeux (MWC) model -- Oxygen Dissociation -- Heterotropic Allosteric Cooperativity -- Homotopic Effect -- Cytochrome c -- Hemochrome Structure -- Absorbance Bands -- Examples -- Electron Transfer in Porphyrins and Metalloporphyrins -- Axial Electron Transfer -- Peripheral Electron Transfer -- Catalases -- Role and Properties -- Reaction Mechanism -- Oxidation Site -- Catalase Mimics -- Peroxidases -- Biological Roles -- Characteristic Features -- Reaction Mechanism -- Model Example -- Models for the Mechanism -- Cytochrome P-450 -- Roles and Main Properties -- Electronic Spectra -- Substrate and Spectral Changes -- Cytochromes P-450 and P-420 -- Catalytic Cycles for P-450 -- P-450 versus HRP -- P-450 versus HRP and Cyt. c Peroxidase -- Electronic Spectra of Hemoproteins -- Optical Transitions of Hemoproteins -- Molecular Orbital and Molecular Energy Wave Functions of Porphyrin Molecule -- π → π Optical Transitions in Hemoproteins -- Molecular Orbitals of Porphyrin Complex -- Electronic Transitions -- Vibronic Excitation -- Symmetry and d-Orbitals -- Electronic Spectra -- ESR Spectra of Hemoproteins -- ESR Spectroscopy and Magnetic Moment -- Symmetry and Splitting Parameters -- Splitting Parameters and g-Values -- High-Spin Ferric Hemoproteins -- Mixed-Spin States in Hemoproteins -- Reduction of Cytochrome c -- Cytochrome P-450 Spectra -- Hyperfine Splitting -- References -- 6 Vitamin B12 -- References -- 7 Chlorophyll -- References -- Index -- End User License Agreement.