Handbook of Green Chemistry, Volume 3: Biocatalysis

Handbook of Green Chemistry, Volume 3: Biocatalysis......Page 1
Contents......Page 2
General Aspects......Page 3
Chemistry of Substrate Oxidation by P450 Monooxygenases......Page 4
Redox Partners of P450 Monooxygenases......Page 6
Major Reactions Catalyzed by P450 Monooxygenases......Page 7
Human P450s in Drug Development......Page 9
Microbial Oxidation for Synthesis of Pharmaceutical Intermediates......Page 10
Plant P450s and Transgenic Plants......Page 12
Replacement or Regeneration of the Cofactor NAD(P)H......Page 14
Engineering of Bacterial P450s......Page 16
Engineering of Mammalian P450s......Page 18
Process Stability of P450s......Page 19
1.4 Outlook......Page 20
References......Page 21
2.1 The Problem with Nitrile Hydrolysis......Page 29
2.2 Biocatalysis as a Green Solution......Page 30
Nitrilase......Page 31
Nitrile Hydratase......Page 32
Chemoselectivity......Page 34
Diastereoselectivity......Page 35
Nicotinamide and Nicotinic Acid......Page 37
Atorvastatin......Page 38
Mandelic Acid......Page 39
1,5-Dimethyl-2-Piperidone, a Lactam......Page 40
3-Hydroxyvaleric Acid......Page 41
Surface Modification of Polymers......Page 42
Biocatalyst Stability......Page 43
Availability......Page 45
2.7 Conclusion......Page 46
References......Page 47
3.1 Introduction......Page 53
Solvent Properties of ILs for Biocatalysis......Page 54
Enzymes in ILs......Page 56
Basic Properties of scCO2......Page 61
Enzymes in scCO2......Page 63
3.4 Biocatalysis in IL–scCO2 Biphasic Systems......Page 65
Phase Behavior of IL–scCO2 Systems......Page 66
Biocatalytic Processes in IL–scCO2 Biphasic Systems......Page 68
3.5 Future Trends......Page 71
References......Page 72
4.1 Introduction......Page 77
Thiamine Diphosphate......Page 78
Lyase and Carboligase Activity Occur at the Same Active Site......Page 81
Chemoselectivity......Page 83
Stereoselectivity......Page 85
Pyruvate Decarboxylases......Page 86
Benzoylformate Decarboxylases......Page 92
Phenylpyruvate Decarboxylases/Indole-3-pyruvate Decarboxylases......Page 93
Benzaldehyde Lyases......Page 94
Mixed Carboligation of Benzaldehyde and Acetaldehyde......Page 96
Self-Ligation of Aliphatic Aldehydes......Page 99
Accessing (S)-2-Hydroxy Ketones......Page 100
Deducing General Principles for Chemo- and Enantioselectivity......Page 102
Donor Binding Site......Page 105
Acceptor Binding Site......Page 106
S-Pockets are Widespread Among ThDP-dependent Enzymes but Not Always
Accessible......Page 107
Carboligation of Two Similar Aldehydes......Page 109
References......Page 110
5.1 Introduction......Page 117
Chemical Versus Enzymatic Baeyer–Villiger Oxidation......Page 118
Catalytic Mechanism......Page 121
Structural Features......Page 122
Isolated Enzymes Versus Whole Cells......Page 123
Baeyer–Villiger Monooxygenases Relevant for Synthetic Applications......Page 126
Kinetic Resolutions of Racemic Ketones......Page 128
Desymmetrization of Prochiral Ketones......Page 132
Regiodivergent Transformations......Page 137
Heteroatom Oxidation......Page 140
5.5 Protein Engineering......Page 142
References......Page 145
6.1 Introduction......Page 153
Classification......Page 154
Sugars as a Hydrogen Source for Reduction......Page 155
Molecular Hydrogen as a Hydrogen Source for Reduction......Page 156
Electric Power as a Hydrogen Source for Reduction......Page 157
Search for the Ideal Biocatalysts......Page 158
Biocatalysts from Screening Techniques......Page 159
Biocatalysts from Recombinant Microorganisms......Page 160
Reaction Systems for Bioreduction......Page 161
Bioreduction Using Whole-Cell Biocatalysts in an Aqueous Solvent......Page 162
Bioreduction Using Whole-Cell Biocatalysts in a Conventional Organic Solvent
and an Aqueous–Organic Solvent......Page 163
Bioreduction Using Whole-Cell Biocatalysts in Supercritical Carbon Dioxide, Ionic Liquids and Fluorous Solvents......Page 166
Bioreduction Using Isolated Enzymes......Page 167
References......Page 169
7.1 Introduction......Page 173
7.2 Small-Molecule Pharmaceuticals......Page 174
7.3 The Concept of Green Chemistry......Page 176
7.4 The Organic Chemistry Toolbox......Page 178
Peptide Synthesis......Page 179
What Should Chemists Consider?......Page 191
7.5 The Enzyme Toolbox (a Selective Analysis)......Page 192
EC 1 Oxidoreductases......Page 193
EC 1.2.1 Dehydrogenases......Page 194
EC 1.14.14 P450 Monooxygenases......Page 196
EC 1.14.13 Baeyer–Villiger Monooxygenases......Page 197
EC 2.4 Glycosyltransferases......Page 198
EC 2.7 Phosphotransferases......Page 199
EC 3 Hydrolases......Page 200
EC 3.1.1.1 Esterases and EC 3.1.1.3 Lipases......Page 201
EC 3.2 Glycosidases......Page 202
EC 3.5 Reactions with C–N Bonds Except Peptide Bonds......Page 203
EC 4.3.1.5 Phenylalanine Ammonia Lyase (PAL)......Page 204
EC 4.1.2 Aldolases......Page 205
EC 4.1.2 Hydroxynitrile Lyases (Oxynitrilases)......Page 207
EC 5 Isomerases......Page 208
7.6 Outlook and Conclusions......Page 209
References......Page 211
8.1 Introduction: The Future Hydrogen Economy......Page 215
Biological Hydrogen Energy Metabolism......Page 217
8.2 Chemistry of Hydrogenase Catalytic Sites......Page 218
NiFe......Page 219
FeFe......Page 221
Fe (non-Fe–S) Hydrogenase (Hmd)......Page 222
8.3 Experimental Approaches......Page 223
FTIR Spectroscopy......Page 224
Protein Film Voltammetry (PFV)......Page 225
8.4 Catalytic Mechanisms of Hydrogenases......Page 226
Fermentation......Page 227
Oxygenic Photosynthesis......Page 228
Anaerobic Photosynthesis......Page 229
Emulation: Hydrogenase Model Compounds......Page 230
Hydrogenases on Electrodes......Page 232
Sensitivity and Resistance of Hydrogenases to O2, CO and Other Inhibitory
Gases......Page 235
8.6 Conclusion and Future Directions......Page 237
References......Page 238
9.1 Introduction......Page 245
9.2 Fate of PAHs in the Environment......Page 246
9.3 Population of PAH-Polluted Environments......Page 248
9.4 Microbial Degradation of PAHs......Page 250
9.5 Dioxygenases as Key Enzymes in the Aerobic Degradation of PAHs and Markers of Bacterial Degradation......Page 253
9.6 PAH Transformation by Extracellular Fungal Enzymes......Page 256
Intrinsic or Natural Attenuation......Page 259
Biostimulation and Bioaugmentation......Page 260
Phytoremediation......Page 263
Feasibility of Bioremediation Technologies......Page 266
References......Page 267