Biochemistry of the Elements
Kluwer Academic / Plenum Publishers (Verlag)
978-0-306-42049-8 (ISBN)
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1. Introduction.- 1.1 Physical Methods.- 1.1.1 Nuclei.- 1.1.2 Electrons.- 1.1.3 Bonding Framework.- 1.1.4 Whole Molecule Methods.- 1.1.5 Kinetic Methods.- 1.2 Probable Future Trends in Physical Instrumentation.- 1.2.1 Double Resonance Methods.- 1.2.2 Dedicated Computers.- References.- 2. Nuclear Magnetic Resonance (Nmr).- 2.1 The Phenomenon.- 2.2 Multinuclear Nmr.- 2.3 Nmr Phenomena Related to Molecular Structure.- 2.3.1 Chemical Shifts.- 2.3.2 Linewidths.- 2.3.3 Spin-Spin Coupling Patterns and Coupling Constants (J).- 2.4 Instrument Characteristics.- 2.4.1 Dispersion.- 2.4.2 Resolution.- 2.4.3 Sensitivity.- 2.4.4 Data Acquisition.- 2.5 Sample Manipulation (Two-Way Communication).- 2.5.1 Multiple Resonance Methods.- 2.5.2 Nuclear Overhauser Effect.- 2.5.3 High-Resolution Nmr Measurements in Crystalline and Liquid Crystalline Phases.- 2.5.4 Spin System Manipulation with Multiple RF Pulses and Cross Polarization.- 2.5.5 Spinning at the "Magic Angle".- 2.5.6 Other Line-narrowing Methods.- 2.6 Biological Considerations.- 2.6.1 Sample Preparation.- 2.6.2 Strong Field Effects.- 2.7 Applications of Nmr to the Biological Elements.- 2.7.1 Nonmetal and Main Group Elements.- 2.7.2 Metal Ions.- 2.7.3 Nmr Spectra of Small Molecules in Binding Interactions with Biopolymers.- 2.7.4 Newer Developments in Nmr.- References.- Appendix A: Correlation Nmr.- Appendix B: Mathematical Symbols Used in Chapter 2.- 3. Nuclear Quadrupole Resonance (Nqr).- 3.1 Properties of Nqr.- 3.2 Relationship to Mossbauer, Esr, and Nmr Spectroscopy.- 3.3 Instrumentation.- 3.4 Applications.- 3.4.1 17O-Nqr.- 3.4.2 Nqr/Infrared Double Resonance.- 3.4.3 Nqr Studies with 14N and 127I.- 3.4.4 Biologically Oriented Studies with 35C1.- 3.4.5 Other Potential Applications of Nqr.- References.- 4. Mossbauer Spectroscopy.- 4.1 Instrumentation.- 4.2 Conversion Electron Detection.- 4.3 Sample Considerations.- 4.4 Mossbauer Effect and the Chemical Environment.- 4.4.1 Isomer Shifts, ? (Also Known as Chemical Shifts).- 4.4.2 Magnetic Effects.- 4.4.3 Quadrupole Splitting (?EQ).- 4.4.4 Linewidth and Lineshape.- 4.5 Biological Applications of 57Fe.- 4.5.1 Iron Porphyrin Structures.- 4.5.2 Nonheme Iron.- 4.5.3 More Complex Entities.- 4.6 Mossbauer Isotopes Other than 57Fe.- 4.7 Mossbauer Emission Spectra.- 4.8 Bragg Scattering Effects.- References.- 5. Electron Spin Resonance (Esr).- 5.1 Introduction.- 5.2 Theory.- 5.2.1 Esr and Molecular Structure.- 5.2.2 Hyperfine Splitting Effects.- 5.2.3 The g-Tensor.- 5.2.4 High-Spin and Low-Spin Complexes.- 5.2.5 Linewidth Effects.- 5.3 Esr Instrumentation.- 5.3.1 Double Resonance Methods: ENDOR.- 5.3.2 ELDOR.- 5.4 Applications.- 5.4.1 Naturally Occurring Ions and Radicals.- 5.4.2 Copper Proteins.- 5.4.3 Esr Studies of Iron: Heme Iron.- 5.4.4 Esr Properties of an Oxidoreductase Containing Both Heme and Nonheme Iron.- 5.4.5 Manganese.- 5.4.6 Isotope Substitutions Which Identify Elements Associated with Paramagnetism.- 5.4.7 Metal Ion Replacements.- 5.4.8 ENDOR Applications.- 5.4.9 Biological Studies with Spin Labels.- 5.4.10 Esr Trends.- References.- 6. X-ray Diffraction Methods for the Analysis of Metalloproteins.- 6.1 Introduction.- 6.1.1 Perspective.- 6.1.2 Scope.- 6.2 Theoretical Basis.- 6.2.1 Crystal Properties.- 6.2.2 Diffraction Theory.- 6.2.3 Structure Factor Equation.- 6.2.4 Electron Density Equation.- 6.3 Experimental Procedures.- 6.3.1 Crystallization.- 6.3.2 Preparation of Heavy-Atom Derivatives.- 6.3.3 Data Measurement.- 6.4 Structural Analysis.- 6.4.1 Phase Determination.- 6.4.2 Map Interpretation and Model Building.- 6.4.3 Refinement.- 6.5 Applications.- References.- 7. Electron Energy Levels: Electron Spectroscopy and Related Methods.- 7.1 Electron Spectroscopy for Chemical Analysis (ESCA) and Ultraviolet Photoelectron Spectroscopy (UPS).- 7.1.1 Instrumentation for Producing Photoelectron Spectra.- 7.1.2 Koopmans' Theorem.- 7.1.3 Empirical Correlations between Atomic Type and Inner Shell Ionization Energy.- 7.1.4 The "Direction" of Binding Energy Shifts in ESCA.- 7.1.5 Correlations between Photoelectron, Nmr, and Mossbauer Chemical Shifts.- 7.1.6 Lineshapes of Photoelectron Energy Levels.- 7.1.7 Sample Requirements for ESCA and UPS.- 7.1.8 Biological Applications of Photoelectron Spectroscopy.- 7.1.9 Core Electron Energies and Shifts in Biomolecules.- 7.1.10 Satellite Peaks.- 7.1.11 Line Intensities.- 7.1.12 Calibration Standards.- 7.1.13 Signal Improvement Methods.- 7.2 Auger (Secondary Electron) Spectroscopy.- 7.2.1 Loss Peaks.- 7.2.2 Auger Electrons.- 7.2.3 Auger Instrumentation.- 7.2.4 Potential Biological Applications of Auger Spectroscopy.- 7.2.5 Auger Imaging Methods (Scanning Auger Microscopy, SAM).- References.- 8. Laser Applications: Resonance Raman (RR) Spectroscopy and Related Methods.- 8.1 Perspective.- 8.2 Resonance Raman (RR) Spectroscopy.- 8.3 Sample Considerations.- 8.4 Symmetry and the Intensity of Vibrational Absorptions.- 8.5 Vibrational Energy Levels.- 8.6 Applications.- 8.6.1 Conventional Raman Spectroscopy (Excitation Away from Absorption Bands).- 8.6.2 Resonance Raman Applications.- 8.7 Newer Methods Which Minimize Fluorescence Interference.- 8.7.1 Coherent Anti-Stokes Raman Spectroscopy (CARS) or Four-Wave Mixing Spectroscopy.- 8.7.2 Time-Resolved Raman Spectroscopy.- References.- 9. Circular Dichroism (CD) and Magnetic Circular Dichroism (MCD).- 9.1 The Relationship between ORD, CD, MORD, and MCD.- 9.1.1 Optical Rotatory Dispersion (ORD).- 9.1.2 Circular Dichroism (CD).- 9.1.3 Magnetic Optical Rotatory Dispersion (MORD) and Magnetic Circular Dichroism (MCD).- 9.2 Sample Considerations.- 9.3 Effects Observed in MCD Spectra.- 9.3.1 A-Term Spectra.- 9.3.2 B-Term Spectra.- 9.3.3 C-Term Spectra.- 9.3.4 MCD Spectra of Optically Active Chromophores.- 9.4 Biochemical Applications.- 9.4.1 Sample Preparations.- 9.4.2 MCD and Heme Structures.- 9.4.3 Iron-Sulfur Cluster Proteins.- 9.4.4 d-Electron Transitions in the Blue Copper Proteins.- 9.4.5 Extrinsic Probes and MCD Effects.- 9.4.6 MCD Studies of Systems Which Do Not Contain Paramagnetic Metal Ions.- References.- 10. Kinetic Methods.- 10.1 Introduction.- 10.2 Methods.- 10.2.1 Flow Techniques.- 10.2.2 Flash Photolysis and Related Techniques.- 10.2.3 Chemical Relaxation Methods.- 10.2.4 Spectroscopic Line Broadening and Lineshape Effects Related to Species Lifetime, the Uncertainty Principle, and Exchange Equilibria.- 10.2.5 Other Kinetic Methods.- 10.2.6 Choice of Detection Methods.- 10.3 Applications.- 10.3.1 Enzyme Kinetics.- 10.3.2 Blue Copper Enzymes.- 10.3.3 In Vivo Kinetic Studies of the Role of Elements.- 10.3.4 Substitution Experiments.- 10.3.5 Paramagnetism.- 10.3.6 Inhibitors.- 10.3.7 Temperature Jump Characterizations.- 10.3.8 Circular Dichroism.- 10.3.9 Chelators.- References.- 11. Bioinorganic Topochemistry: Microprobe Methods of Analysis.- 11.1 Electron Probe Microanalysis.- 11.1.1 Introduction.- 11.1.2 Applications.- 11.2 Ion, Laser, and Proton Microprobe Analysis of Elements.- References.- 12. Neutron Activation Analysis.- 12.1 Introduction.- 12.2 Applications and Examples of Neutron Activation.- References.
Erscheint lt. Verlag | 28.2.1986 |
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Reihe/Serie | Biochemistry of the Elements ; 5 |
Zusatzinfo | biography |
Verlagsort | Dordrecht |
Sprache | englisch |
Themenwelt | Medizin / Pharmazie ► Medizinische Fachgebiete ► Pharmakologie / Pharmakotherapie |
ISBN-10 | 0-306-42049-X / 030642049X |
ISBN-13 | 978-0-306-42049-8 / 9780306420498 |
Zustand | Neuware |
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