Biological Magnetic Resonance. Vol.7

1 NMR Spectroscopy of the Intact Heart.- 1. Introduction.- 2. Experimental Methods.- 2.1. The Perfused Heart.- 2.2. NMR Parameters.- 2.2.1. The Intensity of 31P NMR Signals.- 2.2.2. Changes in Chemical Shifts.- 2.2.3. Saturation Transfer.- 2.3. Methods of Inducing Perturbations in the Perfused Heart.- 3. Applications.- 3.1. Hypoxia.- 3.2. Ischemia.- 3.3. Myocardial Protection.- 3.4. Myocardial Creatine Kinase.- 3.5. Chemical Perturbations.- 3.6. Cardiac Cycle.- 3.7. Respiration.- 3.8. Cardiac Metabolism.- 3.9. In Vivo Detection.- 4. Concluding Remarks.- References.- 2 NMR Methods for Studying Enzyme Kinetics in Cells and Tissue.- 1. Introduction.- 2. Metabolic Pathways.- 3. Measurements of Concentration Changes.- 4. Line Shape, T2 and T1.- 5. Magnetization Transfer.- 5.1. Experimental Methods.- 5.2. Effect of the Equilibrium Constant on Measurements of Exchange.- 5.3. Exchange Pathway.- 5.3.1. Exchange in a Multienzyme System.- 5.3.2. Exchange Catalyzed by a Single Enzyme.- 6. Isotope Exchange.- 6.1. Detection of Isotope Labels by NMR.- 6.2. The Application of Isotopic Labeling in Studies of Enzymes.- 7. Conclusion.- References.- 3 Endor Spectroscopy in Photobiology and Biochemistry.- 1. Introduction.- 2. Principles of Electron-Nuclear Multiple Resonance Spectroscopy.- 2.1. ENDOR in Liquid Solution.- 2.2. TRIPLE Resonance as an Extension of ENDOR in Solution.- 2.3. Experimental Arrangements.- 2.4. Relaxation Theory of ENDOR/TRIPLE in Solution.- 2.5. ENDOR in Liquid Crystals.- 2.6. CIDEP-Enhanced ENDOR.- 2.6.1. Basic Principles.- 2.6.2. CIDEP-Enhanced ENDOR Detection Strategy: Net Effect versus Multiplet Effect.- 2.6.3. Applications of CIDEP-Enhanced ENDOR.- 2.7. ENDOR in Frozen Solution.- 2.7.1. Local ENDOR.- 2.7.2. Matrix ENDOR.- 2.7.3. Distant ENDOR.- 2.8. Electron Spin-Echo ENDOR and Electron Spin-Echo Modulation Spectroscopy.- 3. Representative Examples.- 3.1. Primary Products of Photosynthesis.- 3.1.1. General Remarks.- 3.1.2. Primary Donors in Bacterial Photosynthesis.- 3.1.3. Electron Acceptors in Bacterial Photosynthesis.- 3.1.4. Primary Donors in Plant Photosynthesis.- 3.1.5. Electron Acceptors in Plant Photosynthesis.- 3.2. Hemes and Hemoproteins.- 3.2.1. General Remarks.- 3.2.2. Hemoglobin and Myoglobin.- 3.2.3. Cytochromes.- 3.2.4. Peroxidases.- 3.3. Metalloproteins.- 3.3.1. Copper Proteins.- 3.3.2. Iron-Sulfur Proteins.- 3.3.3. Other Metals in Enzymatic Systems.- 3.4. Flavins and Flavoproteins.- 3.4.1. General Remarks.- 3.4.2. Flavosemiquinone Model Systems.- 3.4.3. Flavosemiquinones in Enzymatic Systems.- 3.5. Other Biologically Active Organic Species.- 3.5.1. Vitamin Quinones.- 3.5.2. Catechols and Catecholamins.- 3.5.3. Phenothiazines.- 4. Summary.- Recent Developments.- References.- 4 NMR Studies of Calcium-Binding Proteins.- 1. Introduction.- 1.1. Calcium Metabolism.- 1.2. Calcium-Binding Proteins.- 1.3. Choice of Suitable NMR Nuclei.- 2. Calcium-43 NMR Studies.- 2.1. Fast Exchange Conditions.- 2.2. Slow Exchange Conditions.- 3. Magnesium-25 NMR Studies.- 4. Cadmium-113 NMR Studies.- 5. Metal Ion Competition Experiments.- 6. Ligand Interactions.- 7. Proton NMR Studies.- 8. Epilogue.- References.