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Metalloproteins comprise approximately 30% of all known proteins, and are involved in a variety of biologically important processes, including oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis, and hydrolysis of amides and esters, environmental sulfur and nitrogen cycles, and disease mechanisms. EPR spectroscopy has an important role in not only the geometric structural characterization of the redox cofactors in metalloproteins but also their electronic structure, as this is crucial for their reactivity. The advent of x-ray crystallographic snapshots of the active site redox cofactors in metalloenzymes in conjunction with high-resolution EPR spectroscopy has provided detailed structural insights into their catalytic mechanisms. This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium) to highlight the importance of high-resolution EPR spectroscopy to the structural (geometric and electronic) characterization of redox active cofactors in metalloproteins. We have been fortunate to have enlisted internationally recognized experts in this joint venture to provide the scientific community with an overview of high-resolution EPR and its application to metals in biology. This volume, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine, covers high-resolution EPR methods, iron proteins, nickel and copper enzymes, and metals in medicine. An eloquent synopsis of each chapter is provided by John Pilbrow in the Introduction. A second volume, Metals in Biology: Applications of High-Resolution EPR to Metalloenzymes, will appear later this year covering the complement of other metalloproteins. One of the pioneers in the development of pulsed EPR and its application to metalloproteins was Arthur Schweiger, whose contribution we include in this volume. Unfortunately, he passed away suddenly during the preparation of this volume. The editors and coauthors are extremely honored to dedicate this volume to the memory of Arthur Schweiger in recognition of his technical advances and insights into pulsed EPR and its application to metalloproteins. Arthur was extremely humble and treated everyone with equal respect. He was a gifted educator with an ability to explain complex phenomena in terms of simple intuitive pictures, had a delightful personality, and continues to be sadly missed by the community. It is an honor for the editors to facilitate the dissemination of these excellent contributions to the scientific community. Suggestions for future volumes are always appreciated.
This unique, self-contained resource is the first volume on electron paramagnetic resonance (EPR) spectroscopy in the eMagRes Handbook series. The 27 chapters cover the theoretical principles, the common experimental techniques, and many important application areas of modern EPR spectroscopy. EPR Spectroscopy: Fundamentals and Methods is presented in four major parts: A: Fundamental Theory, B: Basic Techniques and Instrumentation, C: High-Resolution Pulse Techniques, and D: Special Techniques. The first part of the book gives the reader an introduction to basic continuous-wave (CW) EPR and an overview of the different magnetic interactions that can be determined by EPR spectroscopy, their associated theoretical description, and their information content. The second provides the basics of the various EPR techniques, including pulse EPR, and EPR imaging, along with the associated instrumentation. Parts C and D builds on parts A and B and offer introductory accounts of a wide range of modern advanced EPR techniques, with examples of applications. The last two parts presents most of the new advances that do not appear in most of the classical EPR textbooks that focus on CW EPR. EPR Spectroscopy: Fundamentals and Methods contains, in concise form, all the material needed to understand state-of-the-art EPR spectroscopy at the graduate school/research level, whilst the editors have ensured that it presents the topic at a level accessible to newcomers to the field and others who want to know its range of application and how to apply it.
Metalloproteins comprise approximately 30% of all known proteins, and are involved in a variety of biologically important processes, including oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis, and hydrolysis of amides and esters, environmental sulfur and nitrogen cycles, and disease mechanisms. EPR spectroscopy has an important role in not only the geometric structural characterization of the redox cofactors in metalloproteins but also their electronic structure, as this is crucial for their reactivity. The advent of x-ray crystallographic snapshots of the active site redox cofactors in metalloenzymes in conjunction with high-resolution EPR spectroscopy has provided detailed structural insights into their catalytic mechanisms. This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium) to highlight the importance of high-resolution EPR spectroscopy to the structural (geometric and electronic) characterization of redox active cofactors in metalloproteins. We have been fortunate to have enlisted internationally recognized experts in this joint venture to provide the scientific community with an overview of high-resolution EPR and its application to metals in biology. This volume, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine, covers high-resolution EPR methods, iron proteins, nickel and copper enzymes, and metals in medicine. An eloquent synopsis of each chapter is provided by John Pilbrow in the Introduction. A second volume, Metals in Biology: Applications of High-Resolution EPR to Metalloenzymes, will appear later this year covering the complement of other metalloproteins. One of the pioneers in the development of pulsed EPR and its application to metalloproteins was Arthur Schweiger, whose contribution we include in this volume. Unfortunately, he passed away suddenly during the preparation of this volume. The editors and coauthors are extremely honored to dedicate this volume to the memory of Arthur Schweiger in recognition of his technical advances and insights into pulsed EPR and its application to metalloproteins. Arthur was extremely humble and treated everyone with equal respect. He was a gifted educator with an ability to explain complex phenomena in terms of simple intuitive pictures, had a delightful personality, and continues to be sadly missed by the community. It is an honor for the editors to facilitate the dissemination of these excellent contributions to the scientific community. Suggestions for future volumes are always appreciated.
Metal ions in biology is an ever expanding area in science and medicine involving metal ions in proteins and enzymes, their biosynthesis, catalysis, electron transfer, metal ion trafficking, gene regulation and disease. While X-ray crystallography has provided snapshots of the geometric structures of the active site redox cofactors in these proteins, the application of high resolution EPR spectroscopy in conjunction with quantum chemistry calculations has enabled, in many cases, a detailed understanding of a metalloenzymes mechanism through investigations of the geometric and electronic structure of the resting, enzyme-substrate intermediates and product complexes. This volume, Part II of a two-volume set demonstrates the application of high resolution EPR spectroscopy in determining the geometric and electronic structure of active site metal ion centers in iron sulfur cluster containing metalloproteins, mononuclear molybdenum metalloenzymes, manganese-containing enzymes and novel metalloproteins.
Spin Resonance Spectroscopy: Principles and Applications presents the principles, recent advancements and applications of nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) in a single multi-disciplinary reference. Spin resonance spectroscopic techniques through NMR and EPR are widely used by chemists, physicists, biologists and medicinal chemists. This book addresses the need for new spin resonance spectroscopy content while also presenting the principles, recent advancements and applications of NMR and EPR simultaneously. Ideal for researchers and students alike, the book provides a single source of NMR and EPR applications using a dynamic, holistic and multi-disciplinary approach. Presents a highly interdisciplinary approach by including NMR and EPR applications in chemistry, physics, biology and biotechnology Addresses both NMR and EPR, making its concepts and applications implementable in multiple resonance environments and core scientific disciplines Features a broad range of methods, examples and illustrations for both NMR and EPR to aid in retention and underscore key concepts
The field of Very High Frequency EPR (VHF EPR) or sometimes called Very High Field EPR (conveniently, also abbreviated as VHF EPR) has blossomed during the past decade, especially after the original pioneering work of Ya. S. Lebedev and his group at the Institute of Chemical Physics, Russian Academy of Sciences in Moscow. Although Lebedev suffered heavily under the economic constraints of the communist Soviet Union and then succumbed to cancer at the peak of his scientific career, his groundbreaking work from the 1970's is still considered today to be the 'gold standard' by researchers practicing EPR at high magnetic fields. A stimulus for the production of this book is the legacy of Yakov Levedev in his students now residing in academic positions in the US and elsewhere. The aim of this book is to highlight the state of this growing field. This is an attempt to cover the full scope of VHF EPR in a single volume. The idea for this volume came to the editors at the 2001 Rocky Mountain Analytical Conference during the 24th International EPR Symposium chaired by Sandra and Gareth Eaton. VHF EPR was presented as an independent research field at a workshop organized by LC BruneI and supported by the National High Magnetic Field Laboratory, a National Science Foundation funded facility at Florida State University.
Comprehensive, Up-to-Date Coverage of Spectroscopy Theory and its Applications to Biological SystemsAlthough a multitude of books have been published about spectroscopy, most of them only occasionally refer to biological systems and the specific problems of biomolecular EPR (bioEPR). Biomolecular EPR Spectroscopy provides a practical introduction t
Since its inception 50 years ago, electron paramagnetic resonance (EPR, also called ESR or EMR) has become a major tool in diverse fields ranging from biology and chemistry to solid state physics and materials science. This important book includes personal descriptions of early experiments by pioneers who laid the foundations for the field, perspectives on the state of the art, and glimpses of future opportunities. It presents a broad view of the foundations of EPR and its applications, and will therefore appeal to scientists in many fields. Even the expert will find here history not previously recorded and provocative views of future directions.
This is the first book to summarize the problems of using modern high-resolution 2-mm wave band EPR spectroscopy in an interdisciplinary field for the investigation of various condensed systems. The material is well illustrated and the applications are as diverse as possible. The main subjects included are: unique characteristics of 2-mm EPR spectroscopy and appropriate experimental techniques, dynamics and polarity of radical microenvironment in model and biological systems, and the nature of charge carriers and charge transfer mechanisms in organic polymer semiconductors.
The first volume devoted entirely to Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy This valuable book provides an introduction and broad survey of topics in ESEEM spectroscopy, including the theory, instrumentation, peculiarities of ESE experiments, and analysis of experimental data with particular emphasis on orientationally disordered systems. Applications of ESEEM spectroscopy to study chemically and biologically important paramagnetic centers in single crystals, amorphous solids, and powders are discussed as well. Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy will benefit specialists in magnetic resonance spectroscopy, physicists, chemists, and biologists who use magnetic resonance in their research.