Name: Tetrapyrroles
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ISBN: 9780387785172

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 (H_pD) 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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Tetrapyrroles

9780387785172

0387785175

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