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NMR-Spektroskopie von Nichtmetallen Volume I: Grundlagen, 17O, 33S, 129Xe-NMR-Spektroskopie.
377
However, the advent of new NMR methods like INEPT and inverse detection enables the use of “N NMR for small molecules, even at the level of the natural isotopic abundance. In large molecules such as proteins, an enrichment is demanded. Today “N labeled proteins are imperative for NMR solution structure elucidation. Fortunately, “N enrichment is much less expensive than corresponding r3C enrichment. This Volume 2 in a series of four volumes is mostly devoted to the correlation of the chemical structure and the 15N chemical shifts. More than 60 different classes of N-containing compounds are discussed including isotopic effects on the “N chemical shift. Beyond that, spin-spin couplings of 15N (and 14N) to other nuclei and relaxation of 15N (and r4N) are treated in further chapters. The reader is confronted with a comprehensive presentation of the 15N chemical shift data and the coupling constants. The data are extremely useful for the identification of N-containing compounds. For the eleetrochemist, application to redox systems which can be analyzed qualitatively and quantitatively with the help of 15N NMR are important. The volume contains instructive correlation tables to highlight the structurechemical shift correlations and illustrating figures of titration curves and other correlations. The 15N NMR shifts of several radicals and of ligand complexes are also described. The presentation is very clear, and almost 800 references cover the literature up to 1990. The volume can be recommended for organic chemists who use NMR for structure elucidation and also for NMR researchers as a source of reference. H. FRITZSCHE
Jena
NMR-Spektroskopie von Nichtmetallen Volume I: Grundlagen, “0, 33S, 129XeNMR-Spektroskopie. S. Berger, S. Braun and H.-O. Kalinowski, Georg Thieme Verlag, Stuttgart, 1992, ISBN 3-13-769001-3, xii + 153 pp., DM185.00. The development of nuclear magnetic resonance (NMR) spectroscopy in the last two decades has been characterised by the large application of r3C-resonance in chemistry. The importance of nuclei other than carbon has increased with the possibilities of modern commercial spectrometers. It was necessary to summarise some results from this wide field. Volume I covers the basics of NMR, r70, 33S, and 129Xe NMR spectroscopy. Volumes II-IV describe the spectroscopy of 15N, 31P and 19F. The first volume is divided into six chapters. The first two parts include a short introduction to the theory of the resonance experiment, the experimental technique and a description of the main components of spectrometers with superconducting magnets. An introduction to the many sophisticated methods of 1D and 2D spectroscopy complete this chapter. For non-experts this basic part is a very
378
good explanation of the hardware and related acquisition parameters. Some hints for the preparation of samples and a table of the properties of deuterated solvents close this chapter. Chapter 3 contains a relatively large discussion of the spectral parameters chemical shift, spin-spin coupling and relaxation mechanisms. The theory of each of these parameters is described in clear, understandable detail. Chapters 4-6 are identically structured. First, the general magnetic properties of the isotope are described. The other parts include the topics chemical shifts, coupling constants and relaxation behaviour. “0 spectroscopy is, of course, the largest chapter, with many tables of chemical shifts divided into substance classes of organic chemistry. However, some interesting examples of inorganic applications of “0 spectroscopy are involved. Chapter 5, the sulphur part, involves a table of chemical shifts, good for a first orientation in 33S spectroscopy. The last chapter, ‘29Xe NMR spectroscopy, is a helpful summary of known data especially for chemists in inorganic chemistry. This book is a good introduction for newcomers to the field of NMR spectroscopy of non-metals. It serves well as a starting point for further study and is well documented for additional references. It is strongly recommended for chemists and students who deal with NMR spectroscopy. B. UNDEUTSCH
Jena
Biocoordination Chemistry: Coordination Equilibria in Biologically Active Systems. K. Burger (Editor), Ellis Horwood, Chichester, England, 1990, ISBN 0-13179912-6, 349 pp., $90. Biocoordination Chemistry is one of the most promising fields of inorganic chemistry and an insider can not overview all branches. Therefore such a monograph is welcome. The content of this book concentrates on the complexity of biologically active systems kinetically unstable in solution. The topics addressed are: -acid-base properties of bioligands (B. Noszal), including such general topics as macro, micro and group constants -complexes of amino acids, peptides, and derivatives (I. Sovagu) -The specific influence of metal ions on the amide bond of peptides is described in detail in the chapter on thermodynamics and kinetics of metal complexes with enzymes and proteins (J. Hirose, Y. Kidani) with the exception of porphyrins and similar prosthetic groups (L. Nagy) -metal complexes of carbohydrates (K. Burger) -coordination chemistry of nucleic acid bases and nucleotides (H. Liinnberg).
However, the advent of new NMR methods like INEPT and inverse detection enables the use of “N NMR for small molecules, even at the level of the natural isotopic abundance. In large molecules such as proteins, an enrichment is demanded. Today “N labeled proteins are imperative for NMR solution structure elucidation. Fortunately, “N enrichment is much less expensive than corresponding r3C enrichment. This Volume 2 in a series of four volumes is mostly devoted to the correlation of the chemical structure and the 15N chemical shifts. More than 60 different classes of N-containing compounds are discussed including isotopic effects on the “N chemical shift. Beyond that, spin-spin couplings of 15N (and 14N) to other nuclei and relaxation of 15N (and r4N) are treated in further chapters. The reader is confronted with a comprehensive presentation of the 15N chemical shift data and the coupling constants. The data are extremely useful for the identification of N-containing compounds. For the eleetrochemist, application to redox systems which can be analyzed qualitatively and quantitatively with the help of 15N NMR are important. The volume contains instructive correlation tables to highlight the structurechemical shift correlations and illustrating figures of titration curves and other correlations. The 15N NMR shifts of several radicals and of ligand complexes are also described. The presentation is very clear, and almost 800 references cover the literature up to 1990. The volume can be recommended for organic chemists who use NMR for structure elucidation and also for NMR researchers as a source of reference. H. FRITZSCHE
Jena
NMR-Spektroskopie von Nichtmetallen Volume I: Grundlagen, “0, 33S, 129XeNMR-Spektroskopie. S. Berger, S. Braun and H.-O. Kalinowski, Georg Thieme Verlag, Stuttgart, 1992, ISBN 3-13-769001-3, xii + 153 pp., DM185.00. The development of nuclear magnetic resonance (NMR) spectroscopy in the last two decades has been characterised by the large application of r3C-resonance in chemistry. The importance of nuclei other than carbon has increased with the possibilities of modern commercial spectrometers. It was necessary to summarise some results from this wide field. Volume I covers the basics of NMR, r70, 33S, and 129Xe NMR spectroscopy. Volumes II-IV describe the spectroscopy of 15N, 31P and 19F. The first volume is divided into six chapters. The first two parts include a short introduction to the theory of the resonance experiment, the experimental technique and a description of the main components of spectrometers with superconducting magnets. An introduction to the many sophisticated methods of 1D and 2D spectroscopy complete this chapter. For non-experts this basic part is a very
378
good explanation of the hardware and related acquisition parameters. Some hints for the preparation of samples and a table of the properties of deuterated solvents close this chapter. Chapter 3 contains a relatively large discussion of the spectral parameters chemical shift, spin-spin coupling and relaxation mechanisms. The theory of each of these parameters is described in clear, understandable detail. Chapters 4-6 are identically structured. First, the general magnetic properties of the isotope are described. The other parts include the topics chemical shifts, coupling constants and relaxation behaviour. “0 spectroscopy is, of course, the largest chapter, with many tables of chemical shifts divided into substance classes of organic chemistry. However, some interesting examples of inorganic applications of “0 spectroscopy are involved. Chapter 5, the sulphur part, involves a table of chemical shifts, good for a first orientation in 33S spectroscopy. The last chapter, ‘29Xe NMR spectroscopy, is a helpful summary of known data especially for chemists in inorganic chemistry. This book is a good introduction for newcomers to the field of NMR spectroscopy of non-metals. It serves well as a starting point for further study and is well documented for additional references. It is strongly recommended for chemists and students who deal with NMR spectroscopy. B. UNDEUTSCH
Jena
Biocoordination Chemistry: Coordination Equilibria in Biologically Active Systems. K. Burger (Editor), Ellis Horwood, Chichester, England, 1990, ISBN 0-13179912-6, 349 pp., $90. Biocoordination Chemistry is one of the most promising fields of inorganic chemistry and an insider can not overview all branches. Therefore such a monograph is welcome. The content of this book concentrates on the complexity of biologically active systems kinetically unstable in solution. The topics addressed are: -acid-base properties of bioligands (B. Noszal), including such general topics as macro, micro and group constants -complexes of amino acids, peptides, and derivatives (I. Sovagu) -The specific influence of metal ions on the amide bond of peptides is described in detail in the chapter on thermodynamics and kinetics of metal complexes with enzymes and proteins (J. Hirose, Y. Kidani) with the exception of porphyrins and similar prosthetic groups (L. Nagy) -metal complexes of carbohydrates (K. Burger) -coordination chemistry of nucleic acid bases and nucleotides (H. Liinnberg).