Iron-sulfur clusters in chemistry and biology. Volume 1, Characterization, properties and applications

Volume 1 of the second edition of this book dedicated to iron–sulfur clusters and edited by Tracy Rouault, deals with characterization, properties and applications. Compared with the earlier edition coordinated by the same editor and also published by de Gruyter there are several changes, the most noticeable being that the book has now been split into two different volumes. While I have not yet had the chance to look into the second volume, I have compared this new first volume to the earlier edition. The content has been split in such a way that this first volume deals primarily with physico-chemical properties of iron–sulfur centres and also describes in a very chemistry-oriented way the biochemical mechanisms of a selected number of enzymes (among them biotin synthase, nitrogenase and a number of molybdenum-containing enzymes). Clearly all chapters dealing with the assembly of iron–sulfur clusters have been moved to Volume 2 and hence the reader should not expect much information about this fast developing topic in Volume 1. Compared to the first edition this volume now contains three additional chapters by Noodleman; Guo and Li; and Dodd, Crack, Thomson and Lebrun. The Noodleman chapter deals with quantum chemistry and is possibly a bit redundant but also complementary to an earlier chapter by Ichiye (also present in the new edition and describing the chemical properties of iron–sulfur clusters). The Dodd et al. chapter deals with the reactivity of iron–sulfur clusters with nitric oxide, a most welcome addition in a relatively new field. The other chapters found in this new volume were present in the earlier edition and they include a historical perspective (Bonomi and Rouault), and three chapters discussing various spectroscopic methods for the characterization of ISCs (Guo and Li, Petasis and Hendrich, Chakrabarti and Lindahl). Two additional chapters describe nitrogenase and the discovery of its interstitial carbide from two different perspectives (Sickerman et al., Spatzman et al.). The radical mediated generation of carbon–sulfur bonds is addressed in a chapter on biotin synthase by Jarrett; Hille describes molybdenum-containing enzymes other than nitrogenase; Lanz Squire and Booker detail the role of iron–sulfur clusters in biosynthesis of the lipoyl cofactor; and finally Nicolet and Fontecilla Camps discuss the relationships between ISCs and oxygen. Overall there are thus 13 chapters in this volume. In general, the perspective depends very much on physics and chemistry and thus it is a lot easier to read for physico-chemists than for biologists. It is expected that the second volume should be a lot easier to digest for biologists. Still it is worth the effort of jumping into the orbitals and spins to truly understand the meaning of the EPR Raman and Mössbauer spectra, and in this respect this volume is certainly a lot more detailed than the previous edition. Preface......Page 6 Tracey A. Rouault biography......Page 8 Contents......Page 10 List of contributing authors......Page 18 1. Iron-sulfur proteins: a historical perspective......Page 20 2. Chemistry of iron-sulfur clusters......Page 30 3. From the quantum chemistry of iron-sulfur clusters to redox energetics and reaction pathways in metalloenzymes......Page 40 4. Bioinorganic spectroscopy of iron sulfur proteins— an overview......Page 96 5. Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins......Page 154 6. The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology......Page 182 7. The interstitial carbide of the nitrogenase M-cluster: insertion pathway and possible function......Page 210 8. The iron-molybdenum cofactor of nitrogenase......Page 224 9. Biotin synthase: a role for iron-sulfur clusters in the radical-mediated generation of carbon-sulfur bonds......Page 242 10. Molybdenum-containing iron-sulfur enzymes......Page 268 11. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor......Page 346 12. Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair......Page 378 13. Reactivity of iron-sulfur clusters with nitric oxide......Page 406 Index......Page 458 This volume on iron-sulfur proteins includes chapters that describe the initial discovery of iron-sulfur proteins in the 1960s to elucidation of the roles of iron sulfur clusters as prosthetic groups of enzymes, such as the citric acid cycle enzyme, aconitase, and numerous other proteins, ranging from nitrogenase to DNA repair proteins. The capacity of iron sulfur clusters to accept and delocalize single electrons is explained by basic chemical principles, which illustrate why iron sulfur proteins are uniquely suitable for electron transport and other activities. Techniques used for detection and stabilization of iron-sulfur clusters, including EPR and Mossbauer spectroscopies, are discussed because they are important for characterizing unrecognized and elusive iron sulfur proteins. Recent insights into how nitrogenase works have arisen from multiple advances, described here, including studies of high-resolution crystal structures. This volume on iron-sulfur proteins includes chapters that discuss how microbes, plants, and animals synthesize these complex prosthetic groups, and why it is important to understand the chemistry and biogenesis of iron sulfur proteins. In addition to their vital importance in mitochondrial respiration, numerous iron sulfur proteins are important in maintenance of DNA integrity. Multiple rare human diseases with different clinical presentations are caused by mutations of genes in the iron sulfur cluster biogenesis pathway. Understanding iron sulfur proteins is important for understanding a rapidly expanding group of metabolic pathways important in all kingdoms of life, and for understanding processes ranging from nitrogen fixation to human disease.