J. CHEM. SOC. FARADAY TRANS., 1994, 90(11), 1553-1557 BOOK REVIEWS Reviews in Computational Chemistry. Volume 3. By K. 6. Lipkowitz and D. 6. Boyd. VCH, New York, 1992. Pp. xvi + 271. Price DM 128, f53.ISBN 3-527-89619-8. This is the third volume in an on-going series whose purpose is to provide a resource to help readers keep abreast of devel- opments in computational chemistry. As such, these volumes are designed to be broadly representative of the field. The author of each chapter was asked to provide a mini-tutorial on the computational methods in addition to the usual review article data and references. This volume contains four chapters and a lengthy appendix. Chapter 1 by Tamar Schlick, ‘Optimization Methods in Computational Chemistry’, provides a detailed review of the mathematics of optimization.It contains a general discussion of methods and algorithms, with many references, and also provides several examples of computational chemistry prob- lems. Molecular modelling of deoxycytidine and water cluster geometries are presented. Chapter 2 by Harold A. Scheraga, ‘Predicting Three- dimensional Structure of Oligopeptides’, deals with methods for the prediction of three-dimensional structures of oligopep- tides. It begins by describing how to construct a model of an oligopeptide chain, including potential functions and opti- mization strategies, and it then covers methods for solving the multiple-minimum problem. Applications to simple systems follow. The methods are then extended to larger polypeptides and proteins.25 1 references are cited. Chapter 3 by Andrew E. Torda and Wilfred F. van Gun- steren, ‘Molecular Modelling Using Nuclear Magnetic Res- onance Data’, describes another approach to molecular modelling that uses NMR data. Modelling of experimental NMR data is covered first. This is followed by methods for the adjustment of the three-dimensional coordinates of a molecule to achieve the best agreement between the experi- mental data and known chemical and energetic properties. Chapter 4 by David F. V. Lewis, ‘Computer-Assisted Methods in the Evaluation of Chemical Toxicity ’, deals with computer-assisted methods for the evaluation of chemical toxicity. Methods discussed include QSAR, pattern recogni- tion, computer modelling, and knowledge-based systems.Cytochrome P-450is used as a specific example in conjunc- tion with the COMPACT (computer-optimized molecular parametric analysis of chemical toxicity) method of toxicity investigation. Comparisons of other computer-based systems are also included. A reference list of 227 citations is given. The Appendix is a compendium of software for molecular modelling. Programs that are designed for personal com-puters, minicomputers, workstations, mainframes, and super- computers are all listed, and some of their features are described. In addition, listings of quantum chemistry soft- ware, databases of molecular structures, and molecular graphics and allied methods are given. Said to be the most complete listing of sources of software for computational chemistry that is available, it is a valuable resource.The volumes in this review series, including this one, provide the reader with a compact guide to the world of com- putational chemistry and will be valuable additions to many literature collections. P.C. Jurs Received 25th November, 1993 ~~~~~~ Ion Exchange and Solvent Extraction. Volume 11. Ed. J. A. Marinsky and Y. Marcus. Marcel Dekker, New York, 1993. Pp. xiv + 375. Price $195.00. ISBN 0-8247- 8472-3. In this, the latest volume in an important series, the main topic likely to be of interest to chemists faced with practical problems is the uptake of metals by natural colloids, which are mixtures of hydrous oxides, aluminosilicates, and humic substances, in some cases alive as algae, fungi etc.Chapter four relates metal uptake to the surface structures of such materials, while Chapter six deals with metal-humate inter- actions. These chapters should appeal to those concerned with relevant phenomena in the natural environment, as well as to those who want to exploit natural humic materials in chemical processing. The remaining four chapters treat, from different points of view, the thermodynamics of equilibria between on the one hand, electrolyte solutions, usually in water, but in some cases in, for example, water-acetone mixtures, and on the other, ion exchangers of all kinds, including inter alia resins, inorga- nic exchangers and polyelectrolytes.Chapter one attempts a ‘classical’ thermodynamic approach based on formulae for the activity coefficients of the species in the two phases. This is necessarily exceedingly complicated, and Chapter two makes use, instead, of a three-parameter model, which is able to correlate large quantities of data, but is essentially empiri- cal. Chapter three focuses on the processes at the surface of the solid phase, which are discussed in terms of double-layer theory and of the chemical interactions between the solid surface and the dissolved ions. Chapter five follows a Gibbs- Donnan approach, in which an electrical potential difference between the phases is balanced by a ‘swelling pressure’ in the exchanger phase. These four chapters are by no means easy to follow.In part this is due to the recondite nature of the subject, but the pres- entation adds to the reader’s difficulties. The authors appear to be writing for specialists well versed in the earlier liter- ature, and the editors have not attempted to help the non- specialist, for instance by highlighting the principal features and achievements of each approach and making comparisons between them. In particular in Chapter five, there is no list of symbols and no rigorous definition of the basic concept of swelling pressure. The aim of each of the four chapters is, of course, to explain the results of measurements of ion-exchange equi- libria. Extensive data in this area have long been available and there has been much theorising, but fresh efforts can be justified on the grounds of progress in statistical and com- puter techniques. The authors in all cases demonstrate excel- lent agreement between their theories and the data, though it would be an arduous task to work through the detail of their papers in order to assess the validity of their claims.H. A. C. McKay Received 30th November, 1993 Physico-Chemical Properties of Selected Anionic, Cationic and Nonionic Surfactants. By N. M. Van Os, J. R. Haak and L. A. M. Rupert. Elsevier, Amsterdam, 1993. Pp. viii + 608. Price US $245.75, Dfl. 430.00. ISBN 0-444-89691-0. Although it is difficult to get too enthusiastic about a com- pilation of physico-chemical parameters, the authors have produced an extremely useful and extensive tabulation of the physico-chemical properties of surfactants.It is organised into three chapters; an anionic surfactants (alkyl sulfates, alkane sulfonates and alkylarene sulfonates), cationic sur-factants (alkyl trimethyl ammonium and alkyl pyridinium salts), and non-ionic surfactants (alkyl polyoxyethylene glycol ethers and alkyl phenol (ethylene oxide) ethers. There is an extensive index, which occupies almost a third of the volume. This reflects the thoroughness rather than any redundancy, and does considerably help the reader to quickly access the information sought. The authors have provided a much needed service for those working in the field of surfactants as the compilation goes beyond that of existing works, such as the compilation of cmc’s by Mukerjee and Mysels.However, I suspect that at a price of $245.00 access to the volume may be in many cases restricted just to some libraries; this would be a pity. The authors have not attempted to make this a com-prehensive compilation. The parameters tabulated include c.m.c. krafft temperatures, aggregation number, cloud points, micelle radii, and a range of thermodynamic and other rele- vant parameters. There is no attempt at uniformity of presen- tation, but this does not detract from it’s value. It is difficult at times to decide whether the contents reflects the authors particular needs and interests, or what was readily available in the literature. There are a number of minor criticisms the authors may like to consider, if they ever have the enthusiasm to produce a second edition.The non-ionic phase diagrams included are most welcome, and it was disappointing not to see some for the other surfactant types. There are a few limited references to mixed surfactants. Although this would have added considerably to the length, it is an important area which could have been given more attention. There was a disappointing lack of data on interfacial tension and sur-factant adsorption (from surface tension, surface quasi-elastic light scattering and reflectivity). There were also important classes of surfactants, such as the dialkyl chain surfactants, not included. The practise of including a key to the experi- mental method used in the derivation of some parameters is welcomed, and should have been adopted throughout.Read- ability would have been improved in places if some of the tabulations were simply replaced by a functional form. I was left with the impression that there were not many recent references (say within the last five years), that may just reflect the current nature of publications in this field. However, in conclusion I believe that this is a compilation that most groups working in the field would wish to have access to. J. Penfold Received 20th December, 1993 The World of Physical Chemistry. By K. J. Laidler. Oxford University Press, Oxford, 1993. Pp. xii + 476. Price (Hardcover) f55.00.ISBN 0-19-855597-0. ~ ~~ This book describes the historical development of the main branches of physical chemistry.There are individual chapters on thermodynamics, kinetic theory of gases and statistical mechanics, chemical spectroscopy, electrochemistry, chemical J. CHEM. SOC. FARADAY ’TRANS., 1994, VOL. 90 kinetics, colloid and surface chemistry and quantum chem- istry. Crystallography and several other aspects of structural chemistry are notable omissions in the coverage. The book is written by an eminent reaction kineticist, who has also main- tained throughout his life a strong interest in historical aspects of chemistry; he has published several papers in this area. In these days of domination in physical science by the ultra-specialist and of a general neglect in undergraduate chemistry courses of historical and philosophical aspects, it is refreshing to read a book covering the generalities of physical chemistry, to see how its main facets developed in previous ages and to learn about the people involved in both scientific and personal aspects.In addition to chapters covering the development of the various branches of physical chemistry, there are three introductory chapters on ‘The origins of physical chemistry’, ‘Communication in the physical sciences’, and ‘The growth of the physical sciences’. The first of these covers, inter alia, the difficulty of precise definition of physical chemistry (and indeed of physics and chemistry) and, by an interesting comparison of two eminent reaction kinet- icists (Eyring and Norrish) of the author’s acquaintance, the disparate nature of physical chemists as a breed.In the chap- ters covering developments in particular areas, the contribu- tions of our famous forebears are described in modern terms (and occasionally also in terms used by them at the time). The use of modern terms will make for easier understanding by the reader; those who have read original papers written in the nineteenth century will appreciate the difficulty of under-standing the scientific language of the day. Unfortunately, there are many errors, typographic and otherwise, in the modern terms presentation. I fear that some of these errors reflect inadequate proof reading; additional reading by a col- league, particularly one knowledgeable about modern nota- tions could, I believe, have avoided many of the errors.However, the errors should not detract too much from the general value of the book in its concern with physical chem- ists as people. The historical aspects are well researched and the book is very extensively referenced. In particular substan- tial use has been made of the Dictionary of Scientific Biog- raphy. Both within the main chapters and in an Appendix, there are potted biographies of the many interesting persons (some better known than others) encountered within the book. A few of these are still alive; this is particularly notice- able in the reaction kinetic chapter (where the author’s exper- tise is greatest). Many of the biographies make fascinating reading.One could speculate how some of these scientists might have fared in the present scientific climate; would they have had such broad interest both within physical chemistry and outside science altogether (politics, religion, etc.)? Despite some unfortunate technical errors in the book, I believe that Keith Laidler has made a unique and useful con- tribution to the literature of physical chemistry and I hope that the book will be read widely by physical chemists, chem- istry teachers, students and scientific historians. J. Lee Received 26th January, 1994 ~~ Cambridge Monographs on Atomic, Molecular and Chemical Physics. Photodissociation Dynamics. By R. Schinke. Ed. by A. Dalgarno, P. L. Knight, F. H. Read and R.N. Zare. Cambridge University Press, Cambridge, 1993. Pp. xv + 417. $89.95. ISBN 0-521-38368-4. This is a very nice book. It is clear, well written and broadly based. The intention is not to give a historical description of the understanding of photodissociation dynamics but to present the state of the art of this domain. The content of the book may be broadly described as the application of exact J. CHEM. SOC. FARADAY TRANS., 1994, VOL. 90 and approximate methods of quantum mechanics to the problem. This means that several aspects (in particular the description of experimental techniques) are out of the scope of this book, but experiments are not absent because most of the results of calculations are compared to experimental results.The bibliography is impressive with 700 references, mostly recent, which cover the period of rapid explosion in the field due to the introduction of laser techniques. A brief description is given of the detailed content of this book. The book is divided into 16 chapters, covering 379 pages. The first chapter is an introduction to photo-dissociation, describing the main features and the various interests of this subject. The second chapter treats the quantum description of light absorption, being restricted to the case of single photon processes, and using a classical description of the electromagnetic field. The Born-Oppenheimer approximation is also discussed. The following two chapters present the general treatment with time inde- pendent and time-dependent methods, from basic equations to numerical methods.The classical (i.e. trajectory) descrip- tion of the dynamics is made in Chapter 5. The limiting cases of direct and indirect photodissociation as well as the inter- mediate case are presented in Chapters 6-8, with a descrip- tion of the reflection principle, of resonances and recurrences and of diffuse structures. The question of the vibrational dis- tribution is the focus of Chapter 9 while the rotational dis- tributions are fully described in two long Chapters (10 and 11). The last five chapters treat rather rapidly a series of more specific topics : dissociation of van der Waals molecules, photodissociation of vibrationally excited states, emission spectroscopy of dissociating molecules, non-adiabatic tran-sitions in dissociating molecules and real-time dynamics of photodissociation. This long list gives an impressive view of the content of this book.However, a few subjects concerning the theoretical understanding of photodissociation are not fully described. For instance, this is the case for the anisotropy of the angular momentum distribution of the fragments. A few pages of Chapter 11 discuss the vector correlations, but most of this field is not treated: the word ‘polarization’ is absent from the index, and the seminal van Brunt and Zare paper of 1968 does not appear among the references. To conclude, I am sure that this book will be extremely useful. It will be of interest for a great variety of readers, from graduate students to senior scientists working with molecules.I am not aware of any comparable book on this subject and I think that by its vast content and unified presentation, it will be an almost necessary introduction to photodissociation. J. Vigue Received 26th January, 1994 Biomoleculrr Spectroscopy Part A. Advances In Spectroscopy. Volume 20. Ed. by R. J. H. Clark and R. E. Hester. John Wiley and Sons Ltd, Chichester, 1993.Pp.xxi + 383.Price f120.00.ISBN 0-471-93806-a. The application of spectroscopic methods to the problems of molecular biology, biomolecular spectroscopy, requires the combined expertise of spectroscopists and of their colleagues in the biomedical sciences. This volume describes the work of such groups, usually by their principals, and particularly using various forms of infrared and Raman spectroscopy.It is very noticeable that site-directed mutagenesis is starting to play a large part in many of these spectroscopic and mecha- nistic studies. The absorption of light by the rhodopsins responsible for mammalian vision initiates a photoreaction with a number of intermediates, the dynamics of which cover femtoseconds to seconds. The experimental study of these processes have involved isotope-enriched magic-angle spinning solid-state NMR studies and resonance Raman (RR) measurements. The processes can be slowed by cooling. A third technique involves investigations of the retinal materials using FTIR difference spectroscopy of the membranes.This elegant tech- nique has enable Siebert and his group to show that for bovine rhodopsin a critical link appears to be the 9-methyl group of the chromophore, which somehow transmits (a form of steric trigger) the information of retinal isomerization to the cytosolic loops, causing corresponding conformation changes. Halophilic bacteria such as Halobacterium halobium contain a remarkable light-driven proton pump bacte-riorhodopsin, which enables the organism to synthesize ATP. Infrared difference spectroscopy has been especially useful here, and enables the identification of specific molecular alter- ations vital to proton pumping, and has demonstrated the importance of aspartic acids to the function. Ultraviolet resonance Raman spectroscopy (UVRR) of proteins and related model compounds are reviewed by Spiro’s group.Since an earlier review in 1986 there have been significant improvements in the laser techniques available for these studies, particularly to enable the use of lower laser powers, so avoiding saturation of the signals. UVRR can be used to probe the subtle features of protein tertiary and sec- ondary structures in solution, e.g. to determine helical content, and to probe hydrogen bonding. To achieve this a detailed understanding of the spectra, particularly of the con- stituent chromophores-aromatic amino acid groups (histidine, phenylalanine, tyrosine, tryptophan), of proline, of amide groups, and of simple models such as N-methylacetamide is needed.Studies of hemogloblin dynamics, cytochrome c, myoglobin, bacteriorhodopsin, and of the enzymes ketosteroid isomerase and Cu, Zn-superoxide dismutase are reviewed. FTIR spectroscopic studies of enzyme-substrate complexes have become possible with the advent of modern sensitive FTIR instruments. Similarly RR and FT-Raman studies have benefitted from improvements in laser technology and optoelectronics. Whilst the intensities of FTIR bands are less than the RR bands, and water interferes with the infrared, FTIR is not limited to chromophore-containing groups. Enzyme systems described are serine proteases, nicotinamide adenine dinucleotide linked dehydrogenases, triosephosphate isomerase, phospholipase A, , and ketosteroid isomerase.These spectra techniques can also be used to study protein dynamics. Bakers’ yeast cytochrome c peroxidase (CCP) is a mito- chondrial heme protein that catalyses the reduction of hydrogen peroxide by ferrocytochrome c. Also the gene for CCP has been isolated, cloned, and the protein expressed in Escerichia coli. The latter has enabled delicate structure- function relationships to be established via RR spectroscopy using site-directed mutagenesis techniques. The recombinant protein CCP (MI) and a series of its mutants (Trp -+ Phe; His52 + Leu; Arg48 -,Leu, Lys; His 181 -+ Gly; Asp235 -, Asn; Trpl91 +Phe) have been studied. The mutations allow the coordination of the iron atom [as F~(III) or F~(II)]by surrounding ligands such as histidines and water to be exam-ined in great detail.Combined with EPR and magnetic sus-ceptibility measurements this gives information on the coordinations and spin states at different pHs. It is found that variations in the surrounding side chains of the heme not only alter the spin and coordination state of the heme iron, but also destabilize the delicate architecture of the protein which maintains the mechanical coupling between the proxi- mal and the distal residues. J. CHEM. SOC. FARADAY TRANS., 1994, VOL. 90 Tryptophan is a useful chromophore which occurs in many proteins, in those which do not contain it, then genetically inserted tryptophans can be used as probes without signifi- cant biological and structural modification.The applicability and control of this technique, the measurement of fluores- cence decay lifetimes of the tryptophan residues, and suitable exchanges for tryptophan residues are reviewed. In L-lactate dehydrogenase, succinyl coenzyme A synthetase, glutamine- binding protein, D-a-amino acid transaminase and lac per-mease, the replacement of intrinsic tryptophans to create single tryptophan proteins has been described. Conversely, replacement in non-trytophan containing proteins, or in multi-tryptophan protein where all tryptophans have been replaced, can potentially be used to link biological events, such as catalysis and regulation in enzymes, with shape changes at defined points in proteins of known X-ray struc- ture. The modification experiments are both beautiful and elegant ! Calmodulin (a protein which activates binding of actin and myosin in smooth muscle) has been modified by replacing phenylalanine-99 with tryptophan to help study the multiple calcium binding behaviour.In L-lactate dehydroge- nase the tryptophan fluorescence shows that the closure of the loop of polypeptide carrying the tryptophan probe over the active site of the protein limits the maximum rate of the enzyme. The conformation of the protein at various stages of the reaction cycle in phospholipase A, has been studied using replacement of the single tryptophan by phenylalanine. If flu-orotryptophan is used then ”F NMR can be applied, but here the perturbation of the enzyme function is much greater.Raman microscopy and Raman micro-spectroscopy of single whole cells, with the possibility of spatially resolved monitoring of molecular processes inside a single cell, has become possible with the advent of spectra from samples less than a micrometer spatial resolution. However, current instrumentation limits measurements to cells containing a high concentration of RR scattering material, specific foreign bodies such as crystal-like cellular inclusions, or a very highly condensed protein-DNA complex. Techniques described are confocal Raman spectrometers, UV Raman spectrometers, and Raman microscopes. Great care is needed in the choice of the appropriate spectrometer configuration and also if photochemical cell damage and fluorescence artefacts are to be avoided.Studies so far have been on bacterial cells, eukaryotic cell organelles, algae and plant cells, and animal cells, all showing that a surprising number of possibilities exist for useful measurements. Molecules adsorbed on metal surfaces can show an unusually large Raman cross-section, the change in optical properties near the surface can be detected with the surface- enhanced Raman spectroscopy (SERS) technique. For bio- logically significant molecules the application is about 15 years old, the subject shows particular promise for studying nucleic acids and antitumour drugs, with the study of drug distribution in single living cells, of eye lens pigments in normal and cataractous human eye lens extracts, and influ- enza virus-inhibitor interactions being the most important applications.The technique is likely to become important in biotechnology and in medicine, and where the analysis of large numbers of samples is needed. The final chapter concerns the use of FTIR measurements of the various CH, vibrational modes in phospholipids to try to quantify the conformational disorder in biological mem- branes. This is a new approach which has advantages over X-ray, ESR and NMR measurements, but which needs an order of magnitude gain in infrared sensitivity to be properly exploitable. John Maher Received 26th January, 1994 ~~ ~ Biomolecular Spectroscopy Part B. Advances in Spectroscopy. Volume 21. Ed. by R. J. Clark and R. E. Hester.John Wiley and Sons Ltd, Chichester, 1993. Pp. xix + 344. Price f110.00.ISBN 0-471-93832-7. In this volume, the focus is largely on ultra-fast molecular dynamics. Time-resolved infrared spectroscopy (TRIR) measurements are now possible for events on the picosecond timescale: much of this work has been done in Hochstrasser’s labor- atory. Theory and techniques are described, and the nano to sub-picosecond infrared studies on various proteins so far studied are reviewed. The technique reveals subtle details of the bound CO in the heme-CO complex. For bacte-riorhodopsin the experiments show that it is possible to examine the protein dynamics and the coupling of the chromophore motion to the protein on the picosecond time- scale at ambient temperature.Work on photosynthetic bac- teria is also described. The photoisomerization of the retinylidene chromophore triggers a series of reactions in retinal proteins. The reasons for the particular cis-trans and trans-cis photoionization pathways, which excited state, S, or T,, is involved, why a particular chain length of the conjugated chain is used, and how the protonated Schiff-Base linkage affects the excited- state, are all of fundamental importance. To help answer these questions the excited states of retinoids and aldehyde homologues can be studied by time-resolved, electronic absorption spectroscopy and RR spectroscopy. The tech- niques can also be used to study carotenoids and chlo- rophylls both free and bound in pigment-protein complexes.Carotenoids act both as photo-protectors (preventing forma- tion of singlet oxygen), and as light harvesting materials. For the former the 154s function is selected by the reaction centre probably because of its unique TI-state isomerization property. For the light harvesting function, carotenoids absorb visible light and then transfer this energy to chlo- rophyll with a singlet energy transfer via the 2A, (S,) state. For the chlorophylls changes in the bond orders of the macrocycle on excitation, and intermolecular interactions affect the excited-state properties. Time-resolved RR (TR3) and UVTR3 spectroscopy of pro- teins involves the use of mixing flow cell systems to investi- gate transient species. Combining optical measurements with TR3 enables a check on the species present during the intense laser illumination of the TR3 experiment.An interesting arti- ficial cardiovascular system was used to enable the accumula- tion of spectra of reaction intermediates of cytochrome c oxidase with 0, over a long time using limited amounts of enzyme. The TR3 techniques have been applied to studies of various heme-oxygen systems, e.g. cytochrome P-450, horse radish peroxidase, and cytochrome c oxidase. TR3 has been used to study how ligands such as CO approach the heme iron when they bind to myoglobin. The CO entry probably goes by way of protein rearrangements as distinct from an ‘open’ structure intermediate. TR3 was also used to examine how the quaternary structure of hemoglobin changes on binding/dissociation of CO and how a structural change in the heme ligation in the a-sub-unit can be communicated to the /?-sub-unit. Cytochrome oxidase (CcO) has been estimated to account for 90% of the biological 0, reduction on earth! Much of our knowledge of the dynamics of this system comes from the ‘flash-flow’ techniques first applied by Gibson and Green- wood in 1963.Measurement of transient species by electronic absorption, MCD, TR3, FTIR, TRIK, and RR are reviewed, together with the systems cytochromes aa3, ba,, and 0.The reviewers, (W. H. Woodruff, R. B. Dyer and 0.Einarsdottir) J. CHEM. SOC. FARADAY TRANS., 1994, VOL. 90 present a mechanism for the photodissociation, thermal recombination and thermal dissociation of CcO-CO.This chapter illustrates how difficult it is to speculate on the microscopic mechanism of many metal-enzyme systems, and alongside of this how challenging it is to design experiments to test a mechanism. The theory and measurement of vibrational Raman optical activity (RAO) is reviewed in Chapter 5, its application to biomolecular conformational problems in amino acids, pep- tides, proteins, carbohydrates and nucleosides in aqueous media is described. ROA provides a unique method to inves- tigate the turns, loops and other types of local structure in proteins and small peptides, as well as providing ‘fingerprints’ for complex carbohydrates. In Chapter 6, VCD (vibrational circular dichroism) is described, this com-plements both ECD and RAO, particularly the latter tech- nique. Empirical correlations of VCD spectral features can be made with e.g., the secondary structures of proteins. Instru- mental techniques and sample preparation are described, the latter is critical for VCD since D,O is used for most of the protein measurements. Measurements on polypeptides, oligo- peptides, and nucleic acids are described. Finally the application of X-ray absorption edge spectros- copy (XAS) to the characterization of transition metal sites in biological systems is reviewed. Data for vanadium sites in amavadin and bromoperoxidase, molybdenum in nitro-genase, iron in ferritin and hemosiderin are discussed. In these two volumes, 20 and 21, of the Advances in Spec- troscopy series, the editors, R. J. H. Clark and R. E. Hester have assembled a fascinating summary of the application of (mostly) vibrational spectroscopic studies to biochemistry and bioinorganic chemistry. The articles also provide valu- able summaries of the plethora of new techniques which have arisen as a result of the application of the powerful tri- umvirate of computers, lasers and Fourier transforms ! I suspect that many chemists in other fields of study could find ideas here for applications outside of biochemistry. John Maher Received 26th January, 1994