Springer High Resolution EPR: Applications to Metalloenzymes and Metals in Medicine: 28 (Biological Magnetic Resonance, 28)

This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium). It highlights the importance of high-resolution EPR spectroscopy to the structural characterization of redox active cofactors in metalloproteins. From the Back Cover High Resolution EPR: Applications to Metalloenzymes and Metals in Medicine Prof. Graeme Hanson, University of Queensland and Prof. Lawrence Berliner, University of Denver Metalloproteins are involved in a variety of biologically important processes, including metal ion and oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis and peptide hydrolysis, environmental oxygen, sulphur, and nitrogen cycles, and disease states. High-resolution EPR spectroscopy is crucial in determining the geometric and electronic structural characterization of the redox cofactors in metalloenzymes, which is essential for understanding their reactivity in complex biological systems. This volume, Part I of a two-volume set, covers high-resolution EPR methods, computer simulation, density functional theory, and their application to iron proteins, nickel, and copper enzymes and metals in medicine. The following chapters, written by experts in their fields, include: Advanced Pulse EPR Methods for the Characterization of Metalloproteins: Jeffrey Harmer, George Mitrikas, and Arthur Schweiger Probing Structural and Electronic Parameters in Randomly Oriented Metalloproteins by Orientation-Selective ENDOR Spectroscopy: Reinhard Kappl, Gerhard Bracic, and Jürgen Hüttermann Molecular Sophe: An Integrated Approach to the Structural Characterization of Metalloproteins: The Next Generation of Computer Simulation Software: Graeme Hanson, Christopher Noble, and Simon Benson Spin-Hamiltonian Parameters from First Principle Calculations: Theory and Application: Frank Neese EPR of Mononuclear Non-Heme Iron Proteins: Betty Gaffney Binuclear Non-Heme Iron Enzymes: Nataša Mitic, Gerhard Schenk, and Graeme Hanson Probing the Structure–Function Relationship of Heme Proteins Using Multifrequency Pulse EPR Techniques: Sabine Van Doorslaer EPR Studies of the Chemical Dynamics of NO and Hemoglobin Interactions: Benjamin Luchsinger, Eric Walter, Lisa Lee, Jonathan Stamler, and David Singel EPR Investigation of [NiFe] Hydrogenases: Maurice van Gastel and Wolfgang Lubitz Unique Spectroscopic Features and Electronic Structures of Copper Proteins: Relation to Reactivity: Jungjoo Yoon and Edward Solomon Insulin-Enhancing Vanadium Pharmaceuticals: The Role of Electron Paramagnetic Resonance Methods in the Evaluation of Antidiabetic Potential: Barry Liboiron Chromium in Cancer and Dietary Supplements: Aviva Levina, Rachel Codd, and Peter Lay High-Frequency EPR and ENDOR Characterization of MRI Contrast Agents: Arnold Raitsimring, Andrei Astashkin, and Peter Caravan About the Author Prof. Graeme Hanson, located in the Centre for Magnetic Resonance at the University of Queensland, has applied a unique synergistic approach involving both theoretical and experimental aspects of multifrequency continuous wave and pulsed EPR spectroscopy to structurally (geometric and electronic) characterise the metal binding sites in metalloenzymes and transition metal ion complexes. The development and commercialisation of the XSophe-Sophe-XeprView (CW EPR) and Molecular Sophe(CW EPR, Pulsed EPR and ENDOR) computer simulation software suites has been crucial in the characterisation of these biological inorganic systems.   Dr. Lawrence J. Berliner is currently at the Department of Chemistry and Biochemistry, University of Denver, where he was Professor and Chair for the past 8 years. He retired from The Ohio State University, where he spent a 32-year career in the area of biological magnetic resonance (EPR and NMR). He has been recognized by the International EPR Society with the Silver Medal for Biology/Medicine in 2000. He also received the