Note: Intro -- Historical Development and Perspectives of the Series -- Metal Ions in Life Sciences. -- Preface to Volume 15 -- Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases -- Contents -- Contributors to Volume 15 -- Titles of Volumes 1-44 in the Metal Ions in Biological Systems Series -- Contents of Volumes in the Metal Ions in Life Sciences Series -- Volume 1 Neurodegenerative Diseases and Metal Ions -- Volume 2 Nickel and Its Surprising Impact in Nature -- Volume 3 The Ubiquitous Roles of Cytochrome P450 Proteins -- Volume 4 Biomineralization. From Nature to Application -- Volume 5 Metallothioneins and Related Chelators -- Volume 6 Metal-Carbon Bonds in Enzymes and Cofactors -- Volume 7 Organometallics in Environment and Toxicology -- Volume 8 Metal Ions in Toxicology: Effects, Interactions, Interdependencies -- Volume 9 Structural and Catalytic Roles of Metal Ions in RNA -- Volume 10 Interplay between Metal Ions and Nucleic Acids -- Volume 11 Cadmium: From Toxicity to Essentiality -- Volume 12 Metallomics and the Cell -- Volume 13 Interrelations between Essential Metal Ions and Human Diseases -- Volume 14 The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment -- Volume 15 Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases (this book) -- Volume 16 The Alkali Metal Ions: Their Role for Life (in preparation) -- Chapter 1: The Magic of Dioxygen -- 1 Introduction -- 2 The Rise of Dioxygen in the Atmosphere -- 3 The Dark Side of Dioxygen -- 4 Outlook -- Abbreviations and Definitions -- References -- Chapter 2: Light-Dependent Production of Dioxygen in Photosynthesis -- 1 Introduction -- 2 Geometric and Electronic Structure of the Mn4CaO5 Cluster -- 2.1 Geometric and Electronic Structural Changes During S State Transitions. , 3 X-Ray Diffraction and Spectroscopy of Photosystem II at Room Temperature Using Femtosecond X-Ray Pulses -- 3.1 Simultaneous X-Ray Spectroscopy and Diffraction of Photosystem II -- 3.1.1 X-Ray Emission Spectroscopy of Photosystem II at Room Temperature Using the X-Ray Free Electron Laser -- 3.1.2 X-Ray Diffraction Studies of Photosystem II at Room Temperature Using the X-Ray Free Electron Laser -- 3.2 Intermediate S State Transitions and Mechanism of Dioxygen Evolution -- 3.2.1 X-Ray Free Electron Laser-Based X-Ray Diffraction and X-Ray Emission Spectroscopy of Photosystem II in the S1 and S2 Sta... -- 4 Membrane Inlet Mass Spectrometry and Photosystem II -- 4.1 Membrane Inlet Mass Spectrometry and S State Turnover in X-Ray Free Electron Laser Studies -- 4.2 Time-Resolved Membrane Inlet Mass Spectrometry and Insights into Oxygen Evolution -- 5 Concluding Remarks and Future Directions -- Abbreviations and Definitions -- References -- Chapter 3: Production of Dioxygen in the Dark: Dismutases of Oxyanions -- 1 Introduction -- 2 Geochemistry of the Oxochlorates -- 2.1 Oxochlorates as Respiratory Anions -- 2.2 Natural Abundance of Perchlorate on Earth -- 2.3 Atmospheric and Extraterrestrial Origins of Perchlorate -- 2.4 Perchlorate on Mars -- 3 Perchlorate Respiration -- 3.1 Diversity of Perchlorate-Respiring Microbes -- 3.2 Genetics and Genomics of Perchlorate-Respiring Microbes -- 3.3 (Per)chlorate Reductases -- 3.4 Chlorite Dismutases and Perchlorate Respiration -- 4 Oxygen Generation by Chlorite Dismutases -- 4.1 Structures -- 4.1.1 Primary Structures: Diversity and Hallmarks of O2 Generation -- 4.1.2 Heme-Binding Domain -- 4.1.3 Active Site -- 4.1.4 Tertiary Structures and Oligomerization States -- 4.2 Reactivity and Mechanism -- 4.2.1 Diversity of Reactions Catalyzed by Chlorite Dismutases -- 4.2.2 Possible Pathways for O-O Formation. , 4.2.3 Catalytic Efficiency -- 4.2.4 Reaction Intermediates -- 4.2.5 Structure-Activity Relationships: Highlights -- 4.2.6 Heme and Protein Stability in Diverse Chlorite Dismutase Family Proteins -- 5 Synthetic and Biochemical Models -- 5.1 Chlorite as Reagent with Related Synthetic Metalloporphyrins -- 5.2 Reactions of Chlorite with Horseradish Peroxidase: Implications for Chlorite Dismutases -- 6 General Conclusions -- Abbreviations and Definitions -- References -- Chapter 4: Respiratory Conservation of Energy with Dioxygen: Cytochrome c Oxidase -- 1 Introduction -- 2 The Structures of Bovine Heart Cytochrome c Oxidase -- 2.1 Purification and Crystallization of Bovine Heart Cytochrome c Oxidase -- 2.2 X-Ray Structure of the Protein Moiety -- 2.3 Structure and Stoichiometry of the Metal Sites -- 2.4 Lipid Structures and Contents -- 3 Mechanism of Dioxygen Reduction -- 3.1 Resonance Raman Analysis -- 3.2 X-Ray Structural Data -- 3.3 Biomimetic Studies -- 4 Proton Pump Mechanism -- 4.1 Coupling Between Dioxygen Reduction and Proton Pump -- 4.2 Single Electron Injection Analyses of the Intermediates of the Catalytic Cycle -- 4.2.1 FO Transition -- 4.2.2 The Other Transitions -- 4.3 D-Pathway Mechanism -- 4.3.1 Water-Gated Mechanism -- 4.3.2 Experimental Results Suggesting that Both Chemical and Pumped Protons Are Transferred Through the D-Pathway -- 4.4 H-Pathway Mechanism -- 4.4.1 Structure and Function of the H-Pathway -- 4.4.2 The Structure for Proton Collection and Timely Closure of the Water Channel -- 4.4.3 Mutational Analyses of the H-Pathway -- 4.5 Diversity in Proton Transfer Pathways -- 5 General Conclusions -- Abbreviations and Definitions -- References -- Chapter 5: Transition Metal Complexes and the Activation of Dioxygen -- 1 Introduction -- 1.1 Overview -- 1.2 Paradigm for Dioxygen Activation by Metalloprotein Active Sites. , 2 Dioxygen Activation by Iron Porphyrins -- 2.1 Dioxygen Activation at Heme-Iron Centers: Lessons from Cytochrome P450cam -- 2.2 Iron-Porphyrin Complexes as Heme Models -- 2.2.1 Fe(III)-Superoxo Intermediates -- 2.2.2 Fe(III)-Peroxo Intermediates -- 2.2.3 Fe(III)-Hydroperoxo (Alkylperoxo) Intermediates -- 2.2.4 Fe(IV)-Oxo Intermediates -- 2.2.5 Reactivity of Iron-Porphyrin Intermediates -- Factors Affecting O-O Bond Cleavage: Heterolysis versus Homolysis -- Alkane Hydroxylation by Fe(IV)-Oxo Intermediates -- O-Atom Transfer Reactivity -- Role of the Axial Ligand in Hydroxylation and O-Atom Transfer Reactions -- 2.3 Iron-Porphyrin/Copper Complexes as Cytochrome c Oxidase Models -- 2.3.1 (mu-Peroxo)Iron-Copper Intermediates -- 2.3.2 Reactivity of Iron-Copper Dioxygen Intermediates -- 3 Dioxygen Activation by Non-heme Iron Complexes -- 3.1 Monoiron Models of Mononuclear Non-heme Iron Active Sites -- 3.1.1 Monoiron Superoxo and Hydroperoxo Complexes -- 3.1.2 Monoiron(IV)-Oxo Complexes -- 3.1.3 Monoiron-Cofactor Complexes: Catecholates and α-Ketoglutarates -- 3.2 Diiron Models of Dinuclear Non-heme Diiron Active Sites -- 3.2.1 (Peroxo)diiron Complexes -- 3.2.2 High Valent Diiron-Oxo Complexes -- 4 Dioxygen Activation by Copper Complexes -- 4.1 Mononuclear Models of Monocopper Active Sites in Enzymes -- 4.1.1 1:1 Cu/O2 Adducts -- 4.1.2 CuOOR Complexes -- 4.1.3 Targeting [CuO]+ and Related Monocopper Species -- 4.2 Dicopper Models of Dicopper Active Sites in Enzymes -- 4.2.1 Peroxo- and Bis(mu-oxo)dicopper Complexes -- 4.2.2 (mu-Oxo)dicopper Complexes -- 4.3 Tricopper Models of Multicopper Active Sites in Enzymes -- 5 Concluding Remarks -- Abbreviations and Definitions -- References -- Chapter 6: Methane Monooxygenase: Functionalizing Methane at Iron and Copper -- 1 Introduction -- 2 Particulate Methane Monooxygenase -- 2.1 Architecture -- 2.2 Metal Centers. , 2.3 Identifying the Active Site -- 2.3.1 Proposed Active Sites -- 2.3.2 Evidence for a Dicopper Active Site -- 2.4 Substrate Access and Product Egress from the Dicopper Site -- 2.4.1 Access to the Substrate-Binding Pocket -- 2.4.2 Substrate and Product Channeling -- 2.4.3 Electron Sources -- 2.5 Mechanism -- 2.5.1 Spectroscopic Identification of an Oxygen Intermediate -- 2.5.2 Computational Studies and Comparisons to Copper Model Compounds -- 2.5.3 Mechanism of C-H Bond Breaking -- 2.6 Unresolved Questions -- 3 Soluble Methane Monooxygenase -- 3.1 Genetics and System Components -- 3.1.1 Soluble Methane Monooxygenase -- 3.1.2 Related Bacterial Multicomponent Monooxygenases and Substrate Specificities -- 3.2 Component Structures and Function -- 3.2.1 Soluble Methane Monooxygenase Hydroxylase -- 3.2.2 The Reductase and Electron Transfer to the Hydroxylase -- 3.2.3 The Regulatory Protein and Interactions with the Hydroxylase -- 3.3 The Diiron Center -- 3.3.1 The Oxidized Hydroxylase -- 3.3.2 The Reduced Hydroxylase -- 3.4 Protein Component Complexes -- 3.4.1 Reductase Binding and Effects on the Hydroxylase -- 3.4.2 Hydroxylase Activation by the Regulatory Protein -- 3.4.3 Structures of Regulatory Protein-Hydroxylase Complexes -- 3.4.4 The Activated Soluble Methane Monooxygenase Diiron Center -- 3.4.5 Comparisons to Toluene Monooxygenases and Phenyl Hydroxylase -- 3.5 Substrate Access to the Catalytic Diiron Center -- 3.5.1 Cavities for O2 and Hydrocarbons -- 3.5.2 Proton Delivery -- 3.6 Dimetallic Activation of O2 and Methane -- 3.6.1 Reaction of O2 with the Reduced Hydroxylase -- 3.6.2 Peroxo Intermediates -- 3.6.3 Intermediates Q and Q* -- 3.6.4 The Product-Bound Hydroxylase -- 3.6.5 C-H Bond Activation by Different Intermediates -- 4 Concluding Remarks and Future Directions -- Abbreviations and Definitions -- References. , Chapter 7: Metal Enzymes in ``Impossible´´ Microorganisms Catalyzing the Anaerobic Oxidation of Ammonium and Methane.

Note: Intro -- Historical Development and Perspectives of the Series -- Metal Ions in Life Sciences. -- Preface to Volume 14 -- The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment -- Contents -- Contributors to Volume 14 -- Titles of Volumes 1-44 in the Metal Ions in Biological Systems Series -- Contents of Volumes in the Metal Ions in Life Sciences Series -- Volume 1 Neurodegenerative Diseases and Metal Ions -- Volume 2 Nickel and Its Surprising Impact in Nature -- Volume 3 The Ubiquitous Roles of Cytochrome P450 Proteins -- Volume 4 Biomineralization. From Nature to Application -- Volume 5 Metallothioneins and Related Chelators -- Volume 6 Metal-Carbon Bonds in Enzymes and Cofactors -- Volume 7 Organometallics in Environment and Toxicology -- Volume 8 Metal Ions in Toxicology: Effects, Interactions, Interdependencies -- Volume 9 Structural and Catalytic Roles of Metal Ions in RNA -- Volume 10 Interplay between Metal Ions and Nucleic Acids -- Volume 11 Cadmium: From Toxicity to Essentiality -- Volume 12 Metallomics and the Cell -- Volume 13 Interrelations between Essential Metal Ions and Human Diseases -- Volume 14 The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment (this book) -- Volume 15 Sustaining Life on Planet Earth: Metalloenzymes Mastering Dioxygen and Other Chewy Gases (in press) -- Volume 16 The Alkali Metal Ions: Their Role for Life (in preparation) -- Chapter 1: The Early Earth Atmosphere and Early Life Catalysts -- 1 The Early Earth Atmosphere and Lithosphere -- 1.1 Earth´s Internal Structure -- 2 Catalysts in the Early Earth -- 3 Clays as Possible Catalysts in the Synthesis of Biomolecules -- 4 General Conclusions -- Abbreviations -- References -- Chapter 2: Living on Acetylene. A Primordial Energy Source -- 1 Introduction -- 2 Acetylene -- 2.1 Properties of Acetylene. , 2.2 Sources and Bioavailability of Acetylene on Earth and Other Planets -- 3 Bacteria Living on Acetylene -- 3.1 Pelobacter acetylenicus -- 4 Acetylene Hydratase from Pelobacter acetylenicus -- 4.1 Biochemical and Spectroscopic Properties -- 4.2 Molybdenum-Substituted Enzyme -- 4.3 Crystallization -- 4.4 Structural Overview -- 4.5 Active Site Setup -- 4.6 Site-Directed Mutagenesis -- 4.7 Density Functional Theory Calculations on the Substrate Binding Mode and Amino Acid Protonation States -- 4.8 Towards the Reaction Mechanism -- 5 Conclusions -- Abbreviations and Definitions -- References -- Chapter 3: Carbon Monoxide. Toxic Gas and Fuel for Anaerobes and Aerobes: Carbon Monoxide Dehydrogenases -- 1 Introduction -- 1.1 Chemistry of Carbon Monoxide -- 1.2 Carbon Monoxide in the Biosphere -- 1.2.1 Biological Cycle of Carbon Monoxide -- 1.2.1.1 Sources of Carbon Monoxide -- 1.2.1.2 Removal of Carbon Monoxide -- 1.2.2 Use of Carbon Monoxide under Aerobic and Anaerobic Conditions -- 1.2.2.1 Fates of Carbon Monoxide under Aerobic Conditions -- 1.2.2.2 Fates of Carbon Monoxide under Anaerobic Conditions -- 2 Structure and Function of Carbon Monoxide Dehydrogenases -- 2.1 Cu,Mo-Containing Carbon Monoxide Dehydrogenases -- 2.1.1 Structure of Cu,Mo-Carbon Monoxide Dehydrogenases -- 2.1.2 Spectroscopic Investigations -- 2.1.3 Enzymatic Activity -- 2.1.4 Reaction Mechanism -- 2.2 Monofunctional Ni,Fe-Containing Carbon Monoxide Dehydrogenases -- 2.2.1 Function, Distribution, and Overall Structure -- 2.2.2 Electronic States and Structure of Cluster C -- 2.2.3 Pathways and Channels Involved in Catalysis -- 2.2.4 Inhibited States of Cluster C -- 2.2.5 Mechanism of Reversible Carbon Dioxide Reduction at Cluster C -- 2.3 Bifunctional Ni,Fe-Containing Carbon Monoxide Dehydrogenases -- 2.3.1 Classification and Distribution. , 2.3.2 Structural Characterization of Bacterial CODH/ACS -- 2.3.3 Substrate Binding and Reaction Mechanism -- 2.4 Cu,Mo versus Ni,Fe: Parallels and Differences in Catalytic Strategies -- 3 Concluding Remarks and Future Directions -- Abbreviations -- References -- Chapter 4: Investigations of the Efficient Electrocatalytic Interconversions of Carbon Dioxide and Carbon Monoxide by Nickel-C... -- 1 Direct Carbon Dioxide/Carbon Monoxide Interconversions in Biology -- 2 Nickel-Containing Carbon Monoxide Dehydrogenases -- 3 Protein Film Electrochemistry -- 4 Carbon Monoxide Dehydrogenases as Electrocatalysts -- 4.1 The Electrocatalytic Voltammograms of Class IV Enzymes -- 4.2 The Electrocatalytic Voltammograms of Class III Enzymes -- 5 Potential-Dependent Reactions with Inhibitors -- 5.1 How Class IV Carbon Monoxide Dehydrogenases Respond to Cyanide -- 5.2 How Class IV Carbon Monoxide Dehydrogenases Respond to Cyanate -- 5.3 How Class IV Carbon Monoxide Dehydrogenases Respond to Sulfide and Thiocyanate -- 6 Demonstrations of Technological Significance -- 7 Conclusions -- Abbreviations -- References -- Chapter 5: Understanding and Harnessing Hydrogenases, Biological Dihydrogen Catalysts -- 1 Introduction -- 2 Dihydrogen Cycles and Hydrogenases -- 2.1 The Global Dihydrogen Cycle -- 2.2 Dihydrogen Cycling in Microbial Communities -- 2.3 Solar Dihydrogen Economy -- 2.3.1 Hydrogenase Photoelectrolysis Devices -- 2.3.2 Photosynthetic Dihydrogen -- 3 [NiFe] Hydrogenases -- 3.1 Structure and Function -- 3.1.1 Mechanisms for Dioxygen Tolerance -- 3.1.2 [NiFeSe] Hydrogenases -- 3.2 Biosynthesis -- 4 Nickel-Free Hydrogenases: [FeFe] and [Fe] Enzymes -- 4.1 [FeFe] Hydrogenase Structure and Function -- 4.2 [FeFe] Hydrogenase Biosynthesis -- 4.3 [Fe] Hydrogenases -- 5 Insights into Hydrogenase Mechanism from Small Molecule Mimics -- 6 General Conclusions. , Abbreviations and Definitions -- References -- Chapter 6: Biochemistry of Methyl-Coenzyme M Reductase: The Nickel Metalloenzyme that Catalyzes the Final Step in Synthesis an... -- 1 Introduction -- 1.1 Nickel Enzymes Involved in Metabolism of Environment- and Energy-Relevant Gases -- 1.2 Methyl-Coenzyme M Reductase and Its Involvement in Generation and Utilization of Methane -- 1.3 Ramifications of Methanogenesis in Energy and the Environment -- 1.4 Discoveries Underpinning Recent Studies of Methyl-Coenzyme M Reductase -- 2 Structure and Properties of Methyl-Coenzyme M Reductase and Its Bound Coenzyme F430 -- 2.1 Structure, Properties, and Reactivity of Coenzyme F430 -- 2.2 Structure, Properties, and Reactivity of Methyl-Coenzyme M Reductase -- 3 Redox and Coordination Properties of the Nickel Center in Methyl-Coenzyme M Reductase -- 3.1 Coordination and Oxidation States of the Free F430 Cofactor and Its Pentamethyl Ester Derivative -- 3.2 Coordination and Oxidation States of the Nickel Center -- 4 The Catalytic Mechanism of Methyl-Coenzyme M Reductase -- 5 Summary and Prospects for Future Science and Technology -- Abbreviations -- References -- Chapter 7: Cleaving the N,N Triple Bond: The Transformation of Dinitrogen to Ammonia by Nitrogenases -- 1 Introduction -- 2 The Structural and Biochemical Properties of Mo-Nitrogenase -- 2.1 The Fe Protein and Its Associated Metal Clusters -- 2.1.1 The Polypeptide -- 2.1.2 The [Fe4S4] Cluster -- 2.2 The MoFe Protein and Its Associated Metal Clusters -- 2.2.1 The Polypeptide -- 2.2.2 The P-cluster -- 2.2.3 The FeMoco -- 3 The Catalytic Mechanism of Mo-Nitrogenase -- 3.1 The Thorneley-Lowe Model -- 3.1.1 The Fe Protein Cycle -- 3.1.2 The MoFe Protein Cycle -- 3.2 Further Development and Modifications of the Thorneley-Lowe Model -- 3.2.1 Intermediates of the MoFe Protein Cycle. , 3.2.1.1 The Substrate-Free M4 Intermediate -- 3.2.1.2 The M7 and M8 Intermediates -- 3.2.2 The Reductive Dihydrogen Elimination Mechanism -- 3.2.3 The Alternating Dinitrogen Reduction Pathway -- 4 The Distinct Structural and Catalytic Features of V-Nitrogenase -- 4.1 The Structural Features -- 4.1.1 The Fe Protein -- 4.1.2 The VFe Protein -- 4.2 The Catalytic Features -- 4.2.1 The Reduction of Dinitrogen -- 4.2.2 The Reduction of Carbon Monoxide -- 5 Conclusions -- Abbreviations -- References -- Chapter 8: No Laughing Matter: The Unmaking of the Greenhouse Gas Dinitrogen Monoxide by Nitrous Oxide Reductase -- 1 Introduction: The Biogeochemical Nitrogen Cycle -- 2 Nitrous Oxide: Environmental Effects and Atmospheric Chemistry -- 2.1 Chemical Properties of Dinitrogen Monoxide -- 2.2 Nitrous Oxide, the Greenhouse Effect, and Ozone Depletion -- 2.3 Abiotic and Biotic Sources -- 2.4 Bacterial Denitrification -- 3 Nitrous Oxide Reductase -- 3.1 Anatomy of an Unusual Copper Enzyme -- 3.1.1 Distinct Forms of the Enzyme -- 3.1.2 Three-Dimensional Structures -- 3.2 CuA: More than an Electron Transfer Center -- 3.2.1 Spectroscopic Properties of CuA -- 3.2.2 Three-Dimensional Structure(s) of CuA -- 3.2.3 Unexpected Flexibility: CuA in P. stutzeri Nitrous Oxide Reductase -- 3.3 The Tetranuclear CuZ Center -- 3.3.1 Structural Data on CuZ -- 3.3.2 States of CuZ and Catalytic Properties -- 4 Biogenesis and Assembly of Nitrous Oxide Reductase -- 4.1 The nos Operon -- 4.2 Protein Maturation and CuA Insertion -- 4.3 Assembly of CuZ -- 5 Activation of Nitrous Oxide: The Workings of Nitrous Oxide Reductase -- 5.1 Substrate Access -- 5.2 Gated Electron Transfer -- 5.3 Activation of Nitrous Oxide -- 5.4 The Fate of the Products -- 6 General Conclusions -- Abbreviations and Definitions -- References -- Chapter 9: The Production of Ammonia by Multiheme Cytochromes c. , 1 Introduction.

Note: Ebook , Chapter 1: ORGANOMETALLIC CHEMISTRY OF B12 COENZYMES-- Chapter 2: COBALAMIN- AND CORRINOID-DEPENDENT ENZYMES-- Chapter 3: NICKEL-ALKYL BOND FORMATION IN THE ACTIVE SITE OF METHYL-COENZYME M REDUCTASE-- Chapter 4: NICKEL-CARBON BONDS IN ACETYL-COENZYME A SYNTHASES/CARBON MONOXIDE DEHYDROGENASES-- Chapter 5: STRUCTURE AND FUNCTION OF [NiFe]-HYDROGENASES-- Chapter 6: CARBON MONOXIDE AND CYANIDE LIGANDS IN THE ACTIVE SITE OF [FeFe]-HYDROGENASES-- Chapter 7: CARBON MONOXIDE AS INTRINSIC LIGAND TO IRON IN THE ACTIVE SITE OF [Fe]-HYDROGENASE-- Chapter 8: THE DUAL ROLE OF HEME AS COFACTOR AND SUBSTRATE IN THE BIOSYNTHESIS OF CARBON MONOXIDE-- Chapter 9: COPPER-CARBON BONDS IN MECHANISTIC AND STRUCTURAL PROBING OF PROTEINS AS WELL AS IN SITUATIONS WHERE COPPER IS A CATALYTIC OR RECEPTOR SITE-- Chapter 10: INTERACTION OF CYANIDE WITH ENZYMES CONTAINING VANADIUM, MANGANESE, NON-HEME IRON, AND ZINC-- Chapter 11: THE REACTION MECHANISM OF THE MOLYBDENUM HYDROXYLASE XANTHINE OXIDOREDUCTASE: EVIDENCE AGAINST THE FORMATION OF INTERMEDIATES HAVING METAL-CARBON BONDS-- Chapter 12: COMPUTATIONAL STUDIES OF BIOORGANOMETALLIC ENZYMES AND COFACTORS.