 The Bioinorganic Chemistry of Nickel
ISBN: 978-0-471-18692-2
Hardcover
337 pages
October 1988
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Chapter 1: The Coordination Chemistry of Nickel: An Introductory Survey
1.1. Introduction
1.2. The Element
1.3 Nickel(II) Complexes
1.4. Structure and Bonding
1.5. Ligand Effects
1.6. Four-Coordinate Complexes
1.7. Six-Coordinate Complexes
1.8. Polynuclear Species
1.9. Less Common Oxidation States
1.10. Non-Innocent Ligands
1.11. Dithiolene Complexes
1.12. Dynamic Properties
1.13. Conclusions
References
Chapter 2: Nickel(III) Chemistry and Properties of the Peptide Complexes of Ni(II) and Ni(III)
2.1. Introduction
2.2. Monopeptide Complexes of Nickel (III)
2.3. Bis(dipeptido) Complexes of Nickel(II) and Nickel(III)
2.4. Bis(tripeptido) Complexes of Nickel(III)
2.5. Nickel(III) Mixed-Ligand Complexes
2.6. Electron Transfer and Redox Reactions
References
Chapter 3: The EPR Spectra of Odd-Electron Nickel Ions in Biological Systems: Theory for d7 and d9 Ions
3.1. EPR Spectra of Biological Nickel
3.2. EPR of Nickel in Odd-Electron States
3.3. Crystal Field Theory and the EPR Spectra of d7 and d9 Ions.
3.4. Crystal Field Theory and Low-Symmetry Complexes
3.5. Tetrahedral Complexes
3.6. Conclusions
References
Chapter 4: Electronic and Molecular Structure of Biological Nickel as Studied by X-ray Absorption Spectroscopy
4.1. Introduction
4.2. Nickel Model Compounds
4.3. Nickel Enzymes
References
Chapter 5: Nickel in Biology: Nickel as an Essential Trace Element
5.1. Introduction
5.2. Role of Nickel in Bacteria
5.3. Role of Nickel in Plants
5.4. Role of Nickel in Animals
References
Chapter 6: Biological Transport of Nickel
6.1. Introduction
6.2. Vertebrate Nickel Transport
6.3. Nickel Transport in Plants
6.4. Microbial Nickel Transport
6.5. Nickel Transport by Other Biological Systems
6.6. Conclusions
References
Chapter 7: Urease-A Ni(II) Metalloenzyme
7.1. Historical Perspective
7.2. The Synthesis and Degradation of Urea
7.3. The Nickel Content of Urease and Jackbeans
7.4. Hydroxamic Acids and the Equivalent Weight of Urease
7.5. The Molecular Properties of Urease
7.6. Absorption Spectra
7.7. On the Mechanism of Action of Urease
7.8. Conclusion
References
Chapter 8: Nickel in Hydrogenases from Sulfate-Reducing, Photosynthetic, and Hydrogen-Oxidizing Bacteria
8.1. Introduction
8.2. Structure of Hydrogenases
8.3. Hydrogenase Activity
8.4. Electron Paramagnetic Resonance Spectra
8.5. Redox Properties of Hydrogenases
8.6. The Role of Nickel in Hydrogenase Catalysis
8.7. Concluding Remarks: Toward a Classification of the Nickel-Containing Hydrogenases
References
Chapter 9: (Ni, Fe)Hydrogenases from Sulfate-Reducing Bacteria: Nickel Catalytic and Regulatory Roles
9.1. Introductory Remarks
9.2. Native (Ni, Fe)Hydrogenases
9.3. Intermediate States Generated under H_2 Atmosphere
9.4. Nickel Chemistry in the Context of Its Biological Role
9.5. Mechanism of Hydrogenase Action-Activation and Catalytic Cycles
References
Chapter 10: Hydrogenases of Methanobacterium thermoautotrophicum strain H
10.1. Introduction
10.2. Methanogen Hydrogenases
10.3. Summary
References
Chapter 11: Methyl-S-Coenzyme-M Reductase: A Nickel-Dependent Enzyme Catalyzing the Terminal Redox Step in Methane Biogenesis
11.1. Introduction
11.2. In Vitro Methanogenesis
11.3. F_430
11.4. Electron Microscopy
11.5. Mechanistic Studies of Methyl Reductase
11.5.1. Alternative Substrates and Inhibitors
11.6. Conclusions
References
Chapter 12: Structure and Properties of Coenzyme F_430
12.1. Introduction
12.2. Structure of Coenzyme F_430
12.3. Reactivity at the Ligand Periphery
12.4. Reactivity at the Nickel Center
References
Chapter 13: Carbon Monoxide Dehydrogenase of Acetogens
13.1. Introduction
13.2. Properties of CO Dehydrogenase
13.3. Physiological Role of CO Dehydrogenase
References
Chapter 14: Nickel in CO Dehydrogenase
14.1. Introduction
14.2. CO Dehydrogenase: Physiological Role
14.3. Nickel and CO Chemistry Relating to CO Dehydrogenase Reactions
14.4. Properties of Nickel in CO Dehydrogenase
14.5. Why is Nickel in CO Dehydrogenase?
References
Index
1.1. Introduction
1.2. The Element
1.3 Nickel(II) Complexes
1.4. Structure and Bonding
1.5. Ligand Effects
1.6. Four-Coordinate Complexes
1.7. Six-Coordinate Complexes
1.8. Polynuclear Species
1.9. Less Common Oxidation States
1.10. Non-Innocent Ligands
1.11. Dithiolene Complexes
1.12. Dynamic Properties
1.13. Conclusions
References
Chapter 2: Nickel(III) Chemistry and Properties of the Peptide Complexes of Ni(II) and Ni(III)
2.1. Introduction
2.2. Monopeptide Complexes of Nickel (III)
2.3. Bis(dipeptido) Complexes of Nickel(II) and Nickel(III)
2.4. Bis(tripeptido) Complexes of Nickel(III)
2.5. Nickel(III) Mixed-Ligand Complexes
2.6. Electron Transfer and Redox Reactions
References
Chapter 3: The EPR Spectra of Odd-Electron Nickel Ions in Biological Systems: Theory for d7 and d9 Ions
3.1. EPR Spectra of Biological Nickel
3.2. EPR of Nickel in Odd-Electron States
3.3. Crystal Field Theory and the EPR Spectra of d7 and d9 Ions.
3.4. Crystal Field Theory and Low-Symmetry Complexes
3.5. Tetrahedral Complexes
3.6. Conclusions
References
Chapter 4: Electronic and Molecular Structure of Biological Nickel as Studied by X-ray Absorption Spectroscopy
4.1. Introduction
4.2. Nickel Model Compounds
4.3. Nickel Enzymes
References
Chapter 5: Nickel in Biology: Nickel as an Essential Trace Element
5.1. Introduction
5.2. Role of Nickel in Bacteria
5.3. Role of Nickel in Plants
5.4. Role of Nickel in Animals
References
Chapter 6: Biological Transport of Nickel
6.1. Introduction
6.2. Vertebrate Nickel Transport
6.3. Nickel Transport in Plants
6.4. Microbial Nickel Transport
6.5. Nickel Transport by Other Biological Systems
6.6. Conclusions
References
Chapter 7: Urease-A Ni(II) Metalloenzyme
7.1. Historical Perspective
7.2. The Synthesis and Degradation of Urea
7.3. The Nickel Content of Urease and Jackbeans
7.4. Hydroxamic Acids and the Equivalent Weight of Urease
7.5. The Molecular Properties of Urease
7.6. Absorption Spectra
7.7. On the Mechanism of Action of Urease
7.8. Conclusion
References
Chapter 8: Nickel in Hydrogenases from Sulfate-Reducing, Photosynthetic, and Hydrogen-Oxidizing Bacteria
8.1. Introduction
8.2. Structure of Hydrogenases
8.3. Hydrogenase Activity
8.4. Electron Paramagnetic Resonance Spectra
8.5. Redox Properties of Hydrogenases
8.6. The Role of Nickel in Hydrogenase Catalysis
8.7. Concluding Remarks: Toward a Classification of the Nickel-Containing Hydrogenases
References
Chapter 9: (Ni, Fe)Hydrogenases from Sulfate-Reducing Bacteria: Nickel Catalytic and Regulatory Roles
9.1. Introductory Remarks
9.2. Native (Ni, Fe)Hydrogenases
9.3. Intermediate States Generated under H_2 Atmosphere
9.4. Nickel Chemistry in the Context of Its Biological Role
9.5. Mechanism of Hydrogenase Action-Activation and Catalytic Cycles
References
Chapter 10: Hydrogenases of Methanobacterium thermoautotrophicum strain H
10.1. Introduction
10.2. Methanogen Hydrogenases
10.3. Summary
References
Chapter 11: Methyl-S-Coenzyme-M Reductase: A Nickel-Dependent Enzyme Catalyzing the Terminal Redox Step in Methane Biogenesis
11.1. Introduction
11.2. In Vitro Methanogenesis
11.3. F_430
11.4. Electron Microscopy
11.5. Mechanistic Studies of Methyl Reductase
11.5.1. Alternative Substrates and Inhibitors
11.6. Conclusions
References
Chapter 12: Structure and Properties of Coenzyme F_430
12.1. Introduction
12.2. Structure of Coenzyme F_430
12.3. Reactivity at the Ligand Periphery
12.4. Reactivity at the Nickel Center
References
Chapter 13: Carbon Monoxide Dehydrogenase of Acetogens
13.1. Introduction
13.2. Properties of CO Dehydrogenase
13.3. Physiological Role of CO Dehydrogenase
References
Chapter 14: Nickel in CO Dehydrogenase
14.1. Introduction
14.2. CO Dehydrogenase: Physiological Role
14.3. Nickel and CO Chemistry Relating to CO Dehydrogenase Reactions
14.4. Properties of Nickel in CO Dehydrogenase
14.5. Why is Nickel in CO Dehydrogenase?
References
Index
