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Preface | p. xv |
An Historical Introduction to Porphyrin and Chlorophyll Synthesis | p. 1 |
Historical Introduction to Porphyrins and Porphyrias | p. 1 |
Structure | p. 4 |
The Early Chemical Era | p. 9 |
The Biochemical Descriptive Era | p. 10 |
Early Description of Porphyria | p. 11 |
Classification of Porphyrias | p. 12 |
Enzymes | p. 14 |
Acute Porphyria | p. 15 |
Nonacute Porphyrias | p. 17 |
Porphyria in Animals | p. 18 |
Porphyrin Synthesis in the Animal Kingdom | p. 19 |
The Harderian Gland | p. 19 |
Phototherapy and Cancer | p. 19 |
Retrospective Diagnoses | p. 20 |
Ephemera: Porphyrinurias | p. 21 |
Biosynthesis of 5-Aminolevulinic Acid | p. 29 |
Condensation of Succinyl-CoA and Glycine into Aminolevulinic Acid | p. 29 |
Transfer RNA-Dependent Aminolevulinic Acid Formation | p. 30 |
5-Aminolaevulinic Acid Dehydratase, Porphobilinogen Deaminase and Uroporphyrinogen III Synthase | p. 43 |
5-Aminolaevulinic Acid Dehydratase | p. 43 |
Porphobilinogen Deaminase | p. 58 |
Uroporphyrinogen III Synthase | p. 61 |
Transformation of Uroporphyrinogen III into Protohaem | p. 74 |
Uroporphyrinogen III Decarboxylase | p. 76 |
Coproporphyrinogen III Oxidase/Dehydrogenase | p. 77 |
Protoporphyrinogen IX Oxidase | p. 79 |
Ferrochelatase | p. 81 |
Organization of Pathway | p. 82 |
Inherited Disorders of Haem Synthesis: The Human Porphyrias | p. 89 |
Overview | p. 89 |
Molecular Genetics and Pathogenesis | p. 93 |
Mechanisms of Disease | p. 96 |
New Approaches to Management | p. 97 |
Heme Degradation: Mechanistic and Physiological Implications | p. 101 |
Evolution and Biological Function of Heme Oxygenase | p. 101 |
Sequence and Structural Conservation within the Heme Oxygenase Enzymes | p. 103 |
Crystallographic Studies | p. 103 |
Mechanism of Heme Oxygenase | p. 107 |
Biliverdin Reduction to Bilirubin | p. 110 |
Biliverdin IX¿ Reductase | p. 110 |
Biliverdin IXß Reductase | p. 113 |
Regulation of Mammalian Heme Biosynthesis | p. 116 |
Regulation of Heme Biosynthesis by ALA Synthase | p. 117 |
Regulation at Sites Other Than ALAS | p. 121 |
Tetrapyrroles in Photodynamic Therapy | p. 128 |
Brief History | p. 128 |
Singlet Oxygen: The Cytotoxic Agent | p. 129 |
Singlet Oxygen Targets | p. 129 |
Light Delivery and Requirement | p. 130 |
Photodynamic Damage | p. 130 |
Mechanisms of Tumour and Cellular Uptake | p. 131 |
Tetrapyrroles in Photodynamic Therapy | p. 131 |
Haematoporphyrin Derivative (HpD) and Photofrin | p. 131 |
The Ideal Properties of a Photosensitiser | p. 132 |
Second Generation Photosensitisers | p. 133 |
5,10,15,20 Tetrakis (meso-hydroxphenyl) Chlorin (m-THPC, Foscan, temoporfin) | p. 133 |
5,10,15,20 Tetrakis (meso-hydroxphenyl) Bacteriochlorin (m-THPBC) | p. 134 |
Benzoporphyrin Derivative (BPD, Verteporfin) | p. 135 |
Tin Ethyl Etiopurpurin (SnEt2, Purlytin, Rostaporfin) | p. 136 |
Mono-L-Aspartyl Chlorin e6 (Npe6, MACE, Talaporfin) | p. 136 |
Palladium-Bacteriopheophorbide (TOOKAD, WST009) | p. 137 |
2-[1-hexyloxyethyl]-2-Devinyl Pyropheophorbide-a (HPPH, Photochlor) | p. 138 |
Phthalocyanines | p. 139 |
Lutetium Texaphyrin (Lu-tex, Motexafin Lutetium) | p. 139 |
5-Aminolaevulinic Acid | p. 140 |
Clinical ALA-PDT | p. 141 |
Other Applications of ALA-PDT | p. 141 |
Aminolaevulinic Acid Esters | p. 141 |
Photodetection of Tumours | p. 142 |
Heme Transport and Incorporation into Proteins | p. 149 |
Localization of Heme in Prokaryotes | p. 150 |
Bacterial Heme Transport | p. 151 |
Heme Transport in Eukaryotes | p. 153 |
Unassisted Heme Transport | p. 155 |
Heme-Protein Assembly | p. 155 |
Heme and Hemoproteins | p. 160 |
The Heme Synthetic Pathway | p. 160 |
Structural Variations of the Heme Cofactor | p. 162 |
Heme Iron Coordination in Hemoproteins | p. 165 |
Diversity of Hemoprotein Form and Function | p. 168 |
Spectroscopic Analysis of Hemoproteins | p. 171 |
Novel Aspects and Future Prospects | p. 175 |
Novel Heme-Protein Interactions-Some More Radical Than Others | p. 184 |
Heme as a Sensor: Interactions of Heme with Proteins That Lead to Recognition of Gaseous Molecules: Oxygen, Carbon Monoxide and Nitric Oxide | p. 186 |
Heme Binding to Ion Channels | p. 187 |
Novel Low-Spin Heme-Protein Interactions | p. 188 |
Heme-Binding Proteins That Are Protective, Preventing Heme-Mediated Oxidative Stress | p. 189 |
Heme Transport across Enterocytes and Proof of Principle | p. 193 |
Interactions of Heme with Transcription Factors | p. 195 |
Heme-Protein Interactions and the Control of Circadian Rhythms | p. 196 |
Novel Heme-Protein Interactions for the Control of Intracellular Heme Levels | p. 199 |
Relationships between ATP Concentrations, Oxygen Tension and Heme Transporters, Many of Which Also Interact with Porphyrins | p. 201 |
Synthesis and Role of Bilins in Photosynthetic Organisms | p. 208 |
Structure and Spectral Properties of Protein-Bound Bilins | p. 208 |
Synthesis of Biliverdin IX¿ by Heme Oxygenases | p. 210 |
Biosynthesis of Bilins by Ferredoxin-Dependent Bilin Reductases | p. 212 |
Assembly of Phycobiliproteins and Phytochromes | p. 216 |
The Roles of Bilins in Photosynthetic Organisms | p. 216 |
Phytochromes: Bilin-Linked Photoreceptors in Bacteria and Plants | p. 221 |
The Phytochromes-A Diverse Family of Photoreversible Photoreceptors | p. 222 |
Phytochrome Photosensory Domains | p. 224 |
Physiological Roles of Phytochrome-Like Proteins in Prokaryotes | p. 226 |
Phytochrome Function in Flowering Plants | p. 227 |
Specific Roles for Specific Phytochromes | p. 227 |
Phytochrome Mode of Action | p. 229 |
Phytochrome Regulation of Tetrapyrrole Synthesis | p. 229 |
Biosynthesis of Chlorophyll and Bacteriochlorophyll | p. 235 |
The Insertion of the Central Magnesium Ion | p. 237 |
Methylation of Ring C | p. 238 |
The Missing Link in Chlorophyll Biosynthesis: The Formation of the Isocyclic Ring E of Protochlorophyllide | p. 239 |
Reduction of the 8-Vinyl Group | p. 240 |
Two Routes for the Reduction of Pchlide | p. 241 |
POR: A Light-Driven Enzyme | p. 241 |
DPOR: A Multi-Subunit Enzyme | p. 243 |
The Steps Unique to Bacteriochlorophyll Biosynthesis | p. 244 |
The Final Steps: Addition and Reduction of the Phytol Tail | p. 245 |
Regulation of Tetrapyrrole Synthesis in Higher Plants | p. 250 |
Regulation of the Plant Tetrapyrrole Pathway-At the Heart of Plant Metabolism? | p. 252 |
Turning on the Tap-Regulation of the Synthesis of the Initial Precursor, ALA | p. 253 |
Decision Time at the Branchpoints | p. 256 |
Regulation of the Chlorophyll Branch | p. 258 |
Regulation of the Late Steps of Chlorophyll Biosynthesis | p. 263 |
Light Regulation via NADPH: Protochlorophyllide Oxidoreductase (POR) | p. 264 |
Regulation of Chlorophyll b Biosynthesis | p. 267 |
A New Role for Carotenoids? | p. 269 |
Chlorophyll Breakdown | p. 274 |
Chlorophyll Breakdown in Higher Plants | p. 274 |
Early Steps | p. 275 |
Cleavage of the Chlorophyll Macroring | p. 276 |
The Arrival at Colorless and Nonfluorescent Chlorophyll Breakdown Products | p. 278 |
Breakdown Beyond the Stage of Colorless Tetrapyrrolic Catabolites | p. 280 |
Chlorophyll Catabolites from Other Sources | p. 282 |
Vitamin B12: Biosynthesis of the Corrin Ring | p. 286 |
The First Common Step: Production of Precorrin-2 | p. 287 |
The Aerobic Pathway | p. 288 |
Production of Hydrogenobyrinic Acid | p. 291 |
Proteins of Unknown Function | p. 293 |
The Anaerobic Pathway | p. 293 |
Production of Cobalt-Precorrin-6A | p. 295 |
Conversion of Cobinamide into Coenzyme B12 | p. 300 |
Attachment of 5-Deoxyadenosine, the Upper (Coß) Ligand of Coenzyme B12 | p. 300 |
The Nucleotide Loop Assembly (NLA) Pathway | p. 304 |
The Regulation of Cobalamin Biosynthesis | p. 317 |
The Complexity of Cobalamin | p. 317 |
Cobalamin in Context: Regulating a Branch Point | p. 319 |
Operon Induction and Physiological Significance | p. 321 |
Operon Repression and mRNA Binding | p. 323 |
The Synergy of Cobalamin Transport and Synthesis | p. 324 |
Coenzyme B12-Catalyzed Radical Isomerizations | p. 330 |
Structural Insights into the B12-Dependent Isomerases | p. 331 |
Co-C Bond Activation in B12-Dependent Isomerases | p. 333 |
Radical Flights: Conformational Changes at Play | p. 336 |
Rearrangement Reactions Catalyzed by B12-Dependent Enzymes | p. 338 |
Biosynthesis of Siroheme and Coenzyme F430 | p. 343 |
Siroheme Biosynthesis | p. 343 |
Coenzyme F430 Biosynthesis | p. 346 |
Role of Coenzyme F430 in Methanogenesis | p. 352 |
Methanogenesis | p. 353 |
Free Factor 430 | p. 354 |
Name That Signal | p. 355 |
EPR Signals in Whole Cells | p. 358 |
Structure of MCR and the Nickel Site | p. 360 |
Oxidation State of Nickel in the MCRoxl Form | p. 362 |
Activation and Inactivation of Methyl-Coenzyme M Reductase | p. 363 |
Prelude to the Catalytic Mechanism | p. 366 |
Catalytic Mechanism | p. 367 |
Anaerobic CH4 Oxidation | p. 370 |
MCR Is Still a Mystery | p. 370 |
The Role of Siroheme in Sulfite and Nitrite Reductases | p. 375 |
Siroheme-Containing Sulfite and Nitrite Reductases Represent a Single Enzyme Class | p. 375 |
Diversity between the SiR and NiR Enzymes | p. 377 |
Symmetry Defines Homology between the Assimilatory and Dissimilatory Enzymes | p. 378 |
SiRs and NiRs Have Multiple Redox Centers and Intricate Spectroscopic Features | p. 378 |
X-Ray Crystallographic Structures Support the Spectroscopic Data | p. 378 |
Siroheme Is at the Heart of the Six-Electron Reduction of Sulfite to Sulfide or Nitrite to Ammonia | p. 379 |
Siroheme Anchors the Transformation of Sulfite to Sulfide or Nitrite to Ammonia | p. 381 |
The Siroheme Tetrapyrrole Shows Significant Departure from Planarity | p. 382 |
Siroheme's Structural and Electronic Characteristics Control Anion Interactions | p. 386 |
A Possible ¿ Cation Radical Intermediate | p. 387 |
The Role of Heme d1 in Denitrification | p. 390 |
Structure of Cytochrome cd1 | p. 391 |
Mechanism of Nitrite Reduction | p. 394 |
Insights into d1 heme Chemistry from Model Compound Studies | p. 395 |
Biosynthesis of d1 heme | p. 396 |
Index | p. 401 |
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