INDICE: Chapter 1 1 Introduction Bio–inorganic Chemistry 1 General roles of metal ions in biological system 3 Proteins: Formation, Structure, and Metalloprotins 5 The cell 5 DNA 7 RNA 7 DNA replication 10 mRNA 11 Protein synthesis 12 tRNA 13 Amino acids 14 Polypeptide chains 16 Physiological roles of proteins 16 Primary, secondary, tertiary, quaternary structures and the factors that control each 17 Metalloproteins 23 Enzymes, coenzymes, and cofactors 23 Nicotinamide adenine dinucleitide, NADH 24 Ubiquinone, Coenzyme–Q 24 Flavin mononucleotide, FMN 25 Tetrapyrrolic cofactors, porphyrin, and chlorine 25 Phosphate 26 Comparison between P and S 27 Bioenergetics molecules 28 Suggestions for Further Reading 29 Chapter 2 31 The Alkali and Alkaline Earth Cations Introduction 31 The roles of Na + , and K + in the biological systems 32 The mechanisms for solvent and solute movement through the membrane’s cell 33 Osmosis 34 Passive transport 34 Active transport 36 Na + /K + ATPas 36 Ionophores (antibiotics) and receptors 40 Synthetic ionophores 42 Crown ether 42 Octopus molecule 43 Lariat ether 43 Cryptand ligands 43 Natural ionophores 44 Macrocyclic Esters 44 Macrotetrolides or Actins 44 Depsipeptide macrocycle 44 Valinomycin 44 Carboxylate ionophores 45 Macrocycles 45 Alamethicin 45 Non–macrocycle 46 Nigericin 46 Monensin 46 Dianemycin 46 Antibiotic X–206 46 Antibiotic X–537A 46 Ionophores and metal selection 47 Stereochemistry of metal–ionophores 50 Nerve impulse 53 Magnesium Enzymes 55 DNA– and RNA– polymerase 55 Pyruvate kinase 57 Phosphoglucomutase 60 Creatine kinase 62 Calcium proteins 64 Calsequestrin 64 Parvalbumin 64 Troponin complex 64 Troponin–C 64 Staphylococcal nuclease 65 Thermolysin 65 Concanavalin A 65 Muscle contractions 66 Magnesium and calcium 66 Suggestion for Further Reading 67 Chapter 3 70 Metalloenzymes Introduction 70 Metal–Ions acting as Lewis acids in organic reactions 70 Metal–Ions acting as Lewis acids in biological processes 71 Hydrolysis of ethyl glycinate 71 Decarboxylation of oxaloacetic acid 72 Roles of zinc ions in the biological processes 73 Carboxypeptidases 74 Types of carboxypeptidases 74 Requirements to stimulate carboxypeptidase–A, and carboxypeptidase–B 74 Structural features 75 Zinc ion and reactivity 76 Spectral studies 77 The role of Zn (II) in carboxypeptidase–A, and carboxypeptidase–B 78 Models to mimic the role of the metal ion in carboxypeptidase–A, and carboxypeptidase–B 79 Carbonic Anhydrase 83 Structural and chemical features of carbonic anhydrase 83 The role of the metal ion in carbonic anhydrase 85 Mechanisms that describe the action of carbonic anhydrase 85 Models for the carbonic anhydrase 87 Alcohol Dehydrogenase 88 Role and the chemical structural features of the alcohol dehydrogenase 88 The reaction mechanism of the alcohol dehydrogenase 89 Models for alcohol dehydrogenase 90 Suggestions for further Reading 91 Chapter 4 94 Copper Proteins Introduction 94 Electronic Spectra of Copper Ions 95 Ground state term 95 Electronic spectral selection rules 96 Spectrochemical Series 97 Jahn–Teller effect 98 Symmetry of Cu 2+ –complexes and the electronic spectra 99 Copper(II)–peptide complexes 102 ESR Spectra of Copper Ions 104 The anisotropic effect 106 Isotropic effect 108 The hyperfine and superhyperfine splitting 109 ESR selection rules 111 The g–values 113 A ll –g ll trend 116 Classification of Copper Proteins and significant roles 117 Type–I 120 Plastocyanin 120 Biological function of plastocyanin and the role of the cooper ion 120 The role the polypeptide chain in the biological function of plastocyanin 120 The upper and lower limits of redox potential of the biological systems 121 Factors that may account for the unusual rapid electron transfer in plastocyanin 123 Azurin 127 Stellacyanin 130 Models for plastocyanin 131 Type–II 132 Superoxide Dismutase and the significant role of metal ion 133 Toxicity of superoxide “O 2 ” 134 Structural features of superoxide dismutase 136 Type–III 137 Hemocyanin 137 Structures of the active site 137 Biomimetic model for hemocyanin 130 Multiple–type 141 Ascorbic oxidase and the significant of copper ion 141 Model systems 143 Suggestions for further Reading 144 Chapter 5 148 Iron proteins Introduction 148 Classification of iron proteins 149 Electronic Spectra of Iron Ions 150 Electronic ground states 150 The electronic spectra and the selection role 152 Mössbauer Spectroscopy of Iron Ions 158 Electronic and nuclear resonance absorbance 158 Bases of the Mössbauer spectroscopy 158 Quadrupole splitting 160 Isomer shift 163 ESR Spectra of Iron (III) 165 Advantages of using ESR technique 165 The factors that affect the g–values 166 Iron – Bioavailability 170 Siderophores 175 Role of siderophores 175 Main classes of siderophores 176 The hydroxamates class 176 Ferrichrome family 176 Fluopsin 178 Ferrioxamines family 179 Rhodotorulic acid family 179 Coprogen 180 Aerobactin family 181 Mycobactin family 182 Fusarinine family 182 Phenolate siderophores class 183 2,3–Dihydroxybenzoylglycine (itoic acid) 183 2,3–Dihydroxy–N– benzoyl–L–serine 183 2–N,6–N–Di(2,3–dihydroxybenzoyl)–L–lysine 183 Enterobactin 184 a–Hydroxycarboxylate class 186 Rhizoferrin 186 Mugineic acid 186 Pseudobactin 186 Synthetic siderophores 187 Iron–Storage and Transfer Proteins 188 Ferritin 188 Binding and the release of iron 190 Transferrin 191 Binding Synergism 192 Metal Binding Sites 193 Delivery of iron 193 Mode of ligation influence the Fe 3+ /Fe 2+ redox–cycle 195 The implications of the mode of ligation on the ESR and the electronic spectra 196 Dioxygenase Iron–Proteins 200 Reactions of O 2 –molecule that are catalyzed by metal ion in the biological systems 200 Reaction of organic compounds and oxygen molecules 201 Roles of dioxygenases in the biological systems 201 Intradiol O 2 –ase 202 Extradiol O 2 –ase 202 Catechol–1,2–dioxygenase 202 Protocatechuate–3, 4–dioxygenase (metapyrocatechase) 203 Protocatechuate–4, 5–dioxygenase 204 Protocatechuate–2, 3–dioxygenase 205 Spectroscopic properties of protocatechuate–3, 4–dioxygenase 205 The active site of protocatechuate–3, 4–dioxygenase 205 Mechanism explain the action of dioxygenase 206 Intradiol dioxygenase 208 Extradiol dioxygenase 210 Intradiol versus extradiol 211 Model system 211 Iron–Sulfur Proteins 212 Roles of iron–sulfur proteins 212 Examples of simple and complex iron sulfur proteins 212 Simple iron sulfur proteins Rubredoxin 214 Biological roles, sources, and the main characters 214 Spectroscopic features 215 2Fe–2S Ferredoxins 218 Simplest form, sources, structural, and chemical characteristics 218 Iron atoms and the active–center 219 Sulfur of the active site 220 As valence–trapped dimmer 221 Exchang–coupling, J 222 4Fe–4S Ferredoxins and HiPIP 227 Active site and chemical features 227 “High potential iron sulfur protein”, HiPIP 227 Bacterial ferredoxins, Fd 228 Redox potential 228 Active site analogues 230 Aconitase 232 Biological role 232 Active and inactive forms 232 Reaction mechanism 234 Conjugated Fe–S proteins 235 Hydroxylases 236 Hydroxylases and metabolism 236 Chemical properties 236 Mechanism 238 Hydrogenases 239 Biological role 239 Reactions catalyzed by hydrogenase 240 Ni ion and hydrogenase 241 Structural features 242 Dihydrogen and dihydride complexes 244 Mechanism 245 Nitrogenases 247 Biological role 247 Reaction catalyzed by nitrogenase 247 Unfavorable N 2 –reduction and the possible pathways 248 Structural and nitrogenase components 249 Role of each components 253 Dinitrogen complexes 255 Possible mechanisms for N 2 fixation 257 Binuclear–Fe–Proteins 261 Examples 261 Hemerythrin 261 Sources 261 Comparison among oxygen–carrier proteins 262 Biological characterizations and the chemical forms 262 Oxygen binding 262 Electronic spectra and magnetic studies 266 Mössbauer data of hemerythrin derivatives 267 Ribotide Reductase 269 Function and Requirements 269 Purple acid phosphate 270 Role and reaction mechanism 270 Methane mono–oxygenase 272 Source and role 272 Chemical properties of diiron enzymes 272 Active sites and model compounds 273 Heme proteins; classification and behavior of heme in absence of globins 276 Prosthetics group 276 Examples and biological role 278 General conformations 279 m–Oxo–diiron(III)heme difficulty 280 Myoglobin and hemoglobin 285 Necessity of oxygen carriers 285 Myoglobin 285 Role and main characters 285 Oxymyoglobin and the observed diamagnetism 286 Axial ligand binding and saturation curve 289 Hemoglobin 290 Properties and biological role 290 Oxygen binding 291 Difficulties in the statistical oxygen binding 298 Bohr effect 298 Quaternary structure and oxygen binding 299 Oxygen binding (Adair constants) in term of the allosteric parameters using Monod–Wyman–and Chaneux model 300 Oxygen binding and homotropic interaction 305 Cytochromes 309 Cytochrome–c 309 Biological function and structural features 309 Adduct formation 310 Electronic spectra 310 Redox reactions 312 Electron transfer mechanism 313 Axial electron transfer, requirements 313 Bond cleavage 313 Metal addition 315 Through ligand 316 Peripheral electron transfer, requirements 318 p–Bonding ligands 320 s–Meso addition 321 Catalases 323 Biological role 323 Mechanism 323 Site of oxidation and axial ligand 326 Models 327 Peroxidase 328 Biological role and examples 328 Biological properties of horseradish peroxidase, HRP 329 Route for HRP? action 330 Example of peroxidase reactions 332 Models 333 Cytochrome p–450 335 Role and properties 335 Electronic spectra 337 p–450 and p420 339 Catalytic cycles for p–450 339 p–450 versus HRP and cyto. c peroxidase 340 Examples for the action of p–450 342 Electronic Spectra of Hemoproteins 344 Possible electronic transitions 344 Molecular orbital and the molecular energy wave functions of the porphyrin molecule 345 The p p optical transitions in the hemoproteins 348 Molecular symmetry orbitals for a simplified iron porphyrin complex without axial ligands 349 Characterization of expected electronic transitions 362 Vibronic excitation, b–band (Q v ), in electronic–spectra of hemoprotein?s derivatives 365 Symmetry and 3d orbital of the iron–heme 368 Electronic spectrum of aquomethemoglobin 370 Electronic spectrum of Hb(III)CN 371 Electronic spectrum of Hb(II) 372 Electronic spectrum of Hb(II)CO 373 Electronic spectrum of Hb(II)O 2 374 ESR Spectra of Hemoproteins 376 ESR and magnetic moment 376 Splitting pattern of d–orbital 376 Rhombicity, tetragonal–field and mode of ligation 378 Distortion, spin orbital interaction, applied magnetic field and g–value 381 Mixed–Spin in hemoproteins 385 Two components spin–systems 385 Quantum–mechanically mixed spin system 386 ESR and reduction of cyto.c in alkaline pH 388 ESR and structural description of cytochrome P–450 389 ESR and nitrosyl hemoproteins 390 Suggestions for further reading 393 Chapter 6 405 Vitamin B 12 405 Structural differences among B 12 , B 12r , B 12s , B 12a , and B 12 coenzyme 405 Enzymatic reactions 407 One carbon transfer 407 Formation of methyl mercury from methyl–B 12 407 Formation of methionine from homocysteine 408 Formation of serine from glycine 409 Conversion of CO 2 to acetate 409 The isomerase reactions 409 1,2–shift reactions and examples 409 The reduction of the –CHOH– group of ribonucleotide 412 Possible mechanisms 412 Substrate dissociation and olefin complex formation 412 Substrate dissociation into radical or carbanion 413 Hydrogen cleavage as hydride, hydrogen atom or proton 414 Chemical properties of B 12 416 Model compounds 417 Suggestions for further reading 418 Chapter 7 420 Chlorophyll 420 Chlorophyll and photosynthesis process 420 Molecular structure and role of chlorophyll 421 Light and dark reactions 424 Structure of the chlorophyll serves its function 428 Model for photosynthetic process and synthetic leaf 429 Environments and chlorophyll association 431 Photo–oxidation of chlorophyll 432 Suggestions for further reading 434
- ISBN: 978-1-118-47044-2
- Editorial: Wiley–Blackwell
- Encuadernacion: Rústica
- Páginas: 400
- Fecha Publicación: 14/03/2014
- Nº Volúmenes: 1
- Idioma: Inglés