Biological Magnetic Resonance

Judging from the articles published in Biochemistry, magnetic resonance techniques (NMR and ESR) are now among the most popular methods in biochemical research. The series Biological Magnetic Resonance, the fifth volume of which we are proudly presenting, is intended to provide authori­ tative coverage of topics of current interest. Previous volumes have covered a number of aspects in a thorough and pedagogical fashion rarely found in other publications in this field. Continuing to fulfill the mission of the series, this volume presents a chapter by Baxter, Mackenzie, and Scott on the applications of carbon-13 NMR spectroscopy in investigations of methabolic pathways in vivo. Blom­ berg and Ruterjans give a comprehensive summary of the use of nitrogen-15 NMR in studies of systems of biological interest. Phosphorus-3I NMR investigations of enzyme systems are described by Rao. Tsai and Bruzik outline the principles of and summarize the state-of-the-art advances in the 18 use of oxygen isotopes e 70 and 0) in phosphorus-3I and oxygen-17 NMR studies of biophosphates. Lipid-protein interactions as reflected in ESR and NMR data are discussed by Devaux. We wish to thank the authors for their cooperation in maintaining the and continued high standards of the series.

Inhalt

1 CMR as a Probe for Metabolic Pathways in vivo.- 1. Introduction.- 2. Constraints.- 3. CMR Studies of Metabolic Pathways.- 3.1. Glycolysis and Gluconeogenesis.- 3.2. Gluconeogenesis.- 3.3. Glucose Transport.- 3.4. Porphyrin Biosynthesis.- 3.5. Polyketide Biosynthesis.- 3.6. Mandelic Acid Catabolism.- 3.7. Penicillin Biosynthesis.- 3.8. The Methylmalonate Pathway.- 4. CMR of Metabolism in Whole Organs and Organisms.- 5. Conclusions.- References.- 2 Nitrogen-15 NMR in Biological Systems.- 1. Introduction.- 2. Properties of the Nitrogen NMR Probe.- 2.1. Chemical Shifts.- 2.2. Coupling Constants.- 2.3. Relaxation Processes.- 2.4. Nuclear Overhauser Effect (NOE).- 3. Experimental Techniques.- 4. Amino Acids and Peptides.- 5. Proteins.- 6. Nucleosides, Nucleotides, and Nucleic Acids.- 7. Coenzymes, Antibiotics, and Other Biologically Important Molecules.- 8. 15N NMR of Living Cells and Cell Walls.- 9. Concluding Remarks.- Notation.- References.- 3 Phosphorus-31 Nuclear Magnetic Resonance Investigations of Enzyme Systems.- 1. Introduction.- 2. Basic Considerations.- 2.1. Theoretical.- 2.2. Experimental.- 3. Experimental Results on Specific Enzyme Systems.- 3.1. Hydrolytic Enzymes.- 3.2. Covalently Bound Phosphate Derivates.- 3.3. Experiments with Phosphate Groups with Isotopically Substituted Oxygens.- 3.4. Experiments with Thiophosphate Analogs of Adenine Nucleotides.- 3.5. Enzyme-Bound Substrates, Inhibitors, and Equilibrium Mixtures.- 3.6. Computer Calculation of NMR Line Shapes under the Influence of Exchange.- 3.7. Active Site Structures by Paramagnetic Effects on Relaxation.- 4. Concluding Remarks.- References.- 4 NMR Methods Involving Oxygen Isotopes in Biophosphates.- 1. Introduction.- 2. 18O Isotope Shifts in 31P NMR, S31P_18O.- 3. 17O NMR of Biophosphates.- 3.1. Chemical Shifts.- 3.2. 31P-17O Spin-Spin Coupling Constants, J31P_17O.- 3.3. Linewidths of 17O Resonances.- 4. 31P(17O)NMR.- 4.1. 31P-17O Interactions in Small Biophosphates.- 4.2. 31P-17O Interactions in Macromolecular Systems.- 5. Applications in the Stereochemistry of Enzyme Reactions at Phosphorus.- 5.1. Rationale of Configurational Analysis.- 5.2. Application of 31P(17O) NMR.- 5.3. Application of 31P(18O) NMR.- 5.4. Combination of 31P(17O) and 31P(18O) NMR.- 5.5. Use of 17O NMR in Configurational Analysis.- 6. Other Biochemical Applications.- 6.1. Location and Quantitation of Oxygen or Phosphate.- 6.2. Metal-Nucleotide Interactions.- 6.3. Motional Problems of Phospholipids.- Notation.- References.- 5 ESR and NMR Studies of Lipid-Protein Interactions in Membranes.- 1. Magnetic Resonance and Lipid-Protein Interactions: An Introduction.- 1.1. Overview of Membrane Structure.- 1.2. A Dynamic Description of Biological Membranes: Importance of Magnetic Resonance Studies.- 2. Rotational Diffusion of Membrane Proteins as Influenced by Lipids: Use of Saturation Transfer ESR (ST-ESR).- 2.1. Principles of ST-ESR; Problems Raised by the Application to Anisotropic Motions.- 2.2. Spin-Labeling the Proteins.- 2.3. ST-ESR Studies Applied to the Solubility of Intrinsic Proteins in Lipid Bilayers..- 2.4. Oligomeric Proteins and Spontaneous Protein-Protein Associations.- 2.5. Overall Mobility of the Acetylcholine Receptor Protein in Torpedo marmorata Membrane Fragments : Evidence for Protein-Protein Interactions.- 2.6. Future Applications of ST-ESR to Membranes.- 3. Determination of the " Average Viscosity" of Biological Membranes by Conventional ESR.- 3.1. Spin-Labeling the Lipid Phase.- 3.2. Influence of Proteins on the Rotational Correlation Time of Nitroxides Embedded in the Lipid Phase.- 3.3. Influence of Proteins on the Order Parameter of Spin-Labeled Lipids.- 3.4. Determining the Fraction of Fluid Lipids by the Partitioning of an Amphilic Spin Label.- 3.5. Conclusions.- 4. " Boundary Lipids " of Intrinsic Proteins : Electron Spin Resonance Studies.- 4.1. What is the ESR Spectrum of a Spin-Labeled Phospholipid in Direct Contact with an Intrinsic Protein?.- 4.2. Spin-Labeled Lipids Trapped between Protein Aggregates or Oligomers Give Rise to Broad ESR Components.- 4.3. About the Quantitation of the Fraction of the Immobilized Component in ESR Spectra.- 5. Boundary Lipids of Intrinsic Proteins: 2H NMR Studies.- 5.1. NMR Spectroscopy in Membranes.- 5.2. 2H NMR: Theoretical Background and Experimental Considerations.- 5.3. 2H NMR Investigations of Lipid-Protein Interactions.- 5.4. Conclusions Concerning 2H NMR and Comparison with ESR Views on Boundary Lipids.- 6. Boundary Lipids of Intrinsic Proteins: NMR Studies with 1H, 13C, 19F, or 31P.- 6.1. General Remarks.- 6.2. 1H NMR.- 6.3. 13CNMR.- 6.4. 19FNMR.- 6.5. 31PNMR.- 6.6. Summary of Magnetic Resonance Studies on Boundary Lipids of Intrinsic Membrane Proteins.- 7. Specific Interactions between Lipids and Membrane Proteins. ESR and NMR Studies. Towards an Understanding of the Diversity of Lipid Composition.- 7.1. Specific Interactions between Intrinsic Proteins and Lipids.- 7.2. Specific Interactions between Extrinsic Proteins and Lipids.- 7.3. An NMR Search for Nonbilayer Structures in Model and Biological Membranes.- 8. Concluding Remarks and Future Prospects.- References.