• 1. Introduction — Developments in Enzymatic and Model Studies on Oxygenases.- 1.1. Oxygenases.- 1.2. Oxygenase model s.- 1.3. Biomimetic chemistry and bioinspired catalysis.- 1.4. References.- 2. Dioxygenases.- 2.1. Introduction.- 2.2. Catechol dioxygenases.- 2.3. Other double bond cleaving dioxygenases.- 2.4. Other dioxygenases.- 2.5. Supplement for extradiol cleaving catechol dioxygenases.- 2.6. Concluding remarks.- 2.7. References.- 3. Iron Model Studies on Dioxygenases.- 3.1. Introduction.- 3.2. Catechol dioxygenases.- 3.3. Tryptophan 2,3-dioxygenase.- 3.4. Lipoxygenases.- 3.5. ?-Keto acid-dependent dioxygenases.- 3.6. Supplement for catechol dioxygenases.- 3.7. Concluding remarks.- 3.8. References.- 4. Non-Iron Model Studies on Dioxygenases.- 4.1. Introduction.- 4.2. Cobalt Schiff base complexes as simple dioxygenase models.- 4.3. Co(TPP) catalyzed oxygenation of indoles.- 4.4. Vanadium complexes.- 4.5. Manganese complexes.- 4.6. Copper complexes.- 4.7. Ruthenium, rhodium, iridium complexes.- 4.8. Concluding remarks.- 4.9. References.- 5. Heme Monooxygenases — A Chemical Mechanism for Cytochrome P450 Oxygen Activation —.- 5.1. Introduction.- 5.2. Reaction cycle of cytochrome P450cam.- 5.3. Oxygen bond scission and catalysis.- 5.4. Summary.- 5.5. Acknowledgement.- 5.6. References.- 6. Model Studies on Heme Monooxygenases.- 6.1. Introduction.- 6.2. Successful use of synthetic heme models: Model studies of Fe porphyrin having thiolate ligand.- 6.3. Molecular mechanism of the oxygen activation by P-450.- 6.4. Electrochemical oxidation of iron porphyrin complexes.- 6.5. Mechanistic aspects of compound I formation.- 6.6. O=Mn, O=Cr, and O=Ru porphyrin complexes.- 6.7. Reductive oxygen activation by P-450 models.- 6.8. Catalytic oxidation of organic compoundscatalyzed by iron porphyrins.- 6.9. Catalytic oxidation by manganese porphyrins.- 6.10. Multiplicity of the active species in the catalytic oxidation.- 6.11. Selective oxidations.- 6.12. Metalloporphyrin complexes showing high catalytic efficiency in oxidations.- 6.13. Summary.- 6.14. References.- 7. Nonheme Monooxygenases.- 7.1. Introduction.- 7.2. Nonheme iron monooxygenases.- 7.4. Concluding remarks.- 7.5. References.- 8. Model Studies on Nonheme Monooxygenases — Chemical Models for Nonheme Iron and Copper Monooxygenases —.- 8.1. Introduction.- 8.2. Chemical models for putative reaction intermediates of nonheme iron monooxygenases.- 8.3. Chemical models for copper monooxygenases.- 8.4. References.

' ... the subject is covered in considerable depth and thoroughness and the editor deserves much credit for this. ... the volume is well put together ... has just the right mixture of chemistry and biology to make it of interest and of value to chemists and biochemists alike. I would, therefore, recommend that anybody working in the field should get hold of it, or at least make sure their library has a copy.' Applied Organometallic Chemistry, 12 (1998)