UID:
edocfu_9958126694902883
Format:
1 online resource (272 p.)
ISBN:
1-283-61948-2
,
9786613931931
,
0-08-092386-0
Series Statement:
The porphyrin handbook ; v. 12
Content:
The Porphyrin Handbook
Note:
Description based upon print version of record.
,
Front Cover; The Porphyrin Handbook: The Iron and Cobalt Pigments: Biosynthesis, Structure, and Degradation; Copyright Page; Table of Contents; Preface; Contributors to Volumes 120; Contents of Volumes 1-20; Chapter 69. Regulatory Mechanisms of Eukaryotic Tetrapyrrole Biosynthesis; I. Introduction; II. Differences and Similarities of the Metabolic Pathway in Animals and Plants; III. Control of Mammalian Heme Synthesis; IV. Control of Plant Tetrapyrrole Biosynthesis; V. The Regulatory Network; VI. Conclusion; References; Chapter 70. The Biosynthesis of Coproporphyrinogen III; I. Introduction
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II. The Biosynthesis of 5-Aminolaevulinic AcidIII. The Transformation of 5-Aminolaevulinic Acid into Uroporphyrinogen III; IV. The Transformation of Uroporphyrinogen III into Coproporphyrinogen III; V. Further Conversion of Coproporphyrinogen III into Haem and Alternative Pathways that Transform Uroporphyrinogen III into Precorrin-2, Sirohaem, Factor F4 30 and Vitamin B12; References; Chapter 71. Coproporphyrinogen III and Protoporphyrinogen IX Oxidases; I. Coproporphyrinogen III Oxidase; II. Protoporphyrinogen IX Oxidase; References; Chapter 72. Ferrochelatase; I. Background
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II. Studies on Enzyme ActivityIII. Enzyme Mechanism; IV. Crystal Structures of Ferrochelatases; V. Proposed Enzyme Mechanism; VI. Plant Ferrochelatases; VII. Nonferrochelatase-Catalyzed Metalation; VIII. Mammalian Genomic Organization and Regulation; IX. Erythropoietic Protoporphyria; X. Ferrochelatase and Iron Metabolism; XI. Diversity and Ferrochelatase Evolution; References; Chapter 73. The Family of d-Type Hemes: Tetrapyrroles with Unusual Substituents; I. Introduction; II. Heme d1; III. Hemes d; IV. Honorary d-type Hemes; V. Concluding Remarks; References
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Chapter 74. Biosynthesis and Role of Heme O and Heme AI. Variations in Hemes and Related Compounds; II. Biosynthesis of Heme O; III. Biosynthesis of Heme A; IV. Role of Farnesylated Hemes; V. Organization of Genes Coding the Heme-Copper Terminal Oxidases and Heme O and Heme A Synthases; References; Chapter 75. Heme Oxygenase Structure and Mechanism; I. Introduction; II. Biological Functions of Heme Oxygenase; III. Heme Oxygenase Proteins; IV. Heme Oxygenase Structure; V. Interaction with Cytochrome P450 Reductase and Reductive Reactions; VI. Small Physiological Ligands
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VII. Substrate SpecificityVIII. Heme Oxygenase Model Systems; IX. Stage One: α-meso-Hydroxylation; X. Stage Two: α-meso-Hydroxyheme to Verdoheme; XI. Stage Three: Verdoheme to Biliverdin; XII. Heme Oxygenase Kinetics; XIII. Implications of Electrophilic Heme Oxidation by an Felll-OOH Intermediate; References; Chapter 76. Genetic and Mechanistic Exploration of the Two Pathways of Vitamin B12 Biosynthesis; I. Introduction; II. Genetics of Cobalamin Biosynthesis; III. Comparison of the Aerobic and Anaerobic Pathways to Cobalamin from Aminolevulinic Acid
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IV. Genomics of Cobalamin Biosynthesis - Are there Other Variations in the Route to B12 ?
Additional Edition:
ISBN 0-12-393222-X
Language:
English
