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Title Paramagnetic resonance of metallobiomolecules / Joshua Telser, editor ; sponsored by the ACS Division of Inorganic Chemistry, Inc.
Imprint Washington, D.C. : American Chemical Society, ©2003.

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Description 1 online resource (xi, 432 pages) : illustrations.
Series ACS symposium series ; 858.
ACS symposium series ; 858.
Note Title from PDF title page (ACS publications, viewed Aug 12, 2009).
Bibliog. Includes bibliographical references and indexes.
Note Available only to authorized UTEP users.
English.
Subject Metalloproteins -- Magnetic properties -- Congresses.
Electron paramagnetic resonance -- Congresses.
Metalloproteins -- analysis.
Electron Spin Resonance Spectroscopy.
Electron Spin Resonance Spectroscopy -- history.
Heme Oxygenase (Decyclizing) -- analysis.
Catalysis.
Iron-Sulfur Proteins -- analysis.
Hydrogenase -- analysis.
Molybdoferredoxin -- analysis.
Nitrogenase -- analysis.
Manganese -- analysis.
RNA, Catalytic -- analysis.
Magnetic Resonance Spectroscopy.
Heme -- analysis.
Ferredoxins -- analysis.
Pyrococcus furiosus -- chemistry.
Isomerism.
Metals -- analysis.
Circular Dichroism.
Pterins -- analysis.
Genre Conference papers and proceedings.
Electronic books.
Contents Paramagnetic Resonance of Metallobiomolecules: Introduction and Overview / Telser, Joshua / http://dx.doi.org/10.1021/bk-2003-0858.ch001 -- Electron Spin Echo Methods: A Tutorial / Britt, R. David / http://dx.doi.org/10.1021/bk-2003-0858.ch002 -- Past, Present, and Future of Orientation-Selected ENDOR Analysis: Solving the Challenges of Dipolar-Coupled Nuclei / Doan, Peter E. / http://dx.doi.org/10.1021/bk-2003-0858.ch003 -- Effects of Electron Spin Delocalization and Non-Collinearity of Interaction Terms in EPR Triplet Powder Patterns / Mansoorabadi, Steven O.; Reed, George H. / http://dx.doi.org/10.1021/bk-2003-0858.ch004 -- EPR Characterization of the Heme Oxygenase Reaction Intermediates and Its Implication for the Catalytic Mechanism / Ikeda-Saito, Masao, Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Katahira, Aoba, Sendai 980-8577, Japan, Current address: Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106-4970; Fujii, Hiroshi, Institute for Molecular Science, Okazaki 444-8585, Japan, Current address: Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106-4970 / http://dx.doi.org/10.1021/bk-2003-0858.ch005 -- Paramagnetic Resonance in Mechanistic Studies of Fe-S/Radical Enzymes / Broderick, Joan B., Department of Chemistry, Michigan State University, East Lansing, MI 48864; Walsby, Charles, Department of Chemistry, Northwestern University, Evanston, IL 60203; Broderick, William E., Department of Chemistry, Michigan State University, East Lansing, MI 48864; Krebs, Carsten, Department of Physics, Emory University, Atlanta, GA 30322; Hong, Wei, Department of Chemistry, Michigan State University, East Lansing, MI 48864; Ortillo, Danilo, Department of Chemistry, Michigan State University, East Lansing, MI 48864; Cheek, Jennifer, Department of Chemistry, Michigan State University, East Lansing, MI 48864; Huynh, Boi Hanh, Department of Physics, Emory University, Atlanta, GA 30322; Hoffman, Brian M., Department of Chemistry, Northwestern University, Evanston, IL 60203 / http://dx.doi.org/10.1021/bk-2003-0858.ch006 -- EPR and ENDOR Studies of [NiFe] Hydrogenase: Contributions to Understanding the Mechanism of Biological Hydrogen Conversion / Lubitz, Wolfgang, Max-Planck-Institut für Strahlenchemie, Stiftstraße 34-36, D-45470 Mülheim an der Ruhr, Germany; Brecht, Marc, Max-Volmer-Laboratorium für Biophysikalische Chemie, Fakultät für Mathematik und Naturwissenschaften, Technische Universität Berlin, Straße des 17, Juni 135, D-10623 Berlin, Germany; Foerster, Stefanie, Max-Volmer-Laboratorium für Biophysikalische Chemie, Fakultät für Mathematik und Naturwissenschaften, Technische Universität Berlin, Straße des 17, Juni 135, D-10623 Berlin, Germany; Gastel, Maurice van, Max-Planck-Institut für Strahlenchemie, Stiftstraße 34-36, D-45470 Mülheim an der Ruhr, Germany; Stein, Matthias, Max-Volmer-Laboratorium für Biophysikalische Chemie, Fakultät für Mathematik und Naturwissenschaften, Technische Universität Berlin, Straße des 17, Juni 135, D-10623 Berlin, Germany / http://dx.doi.org/10.1021/bk-2003-0858.ch007 -- Q-Band ENDOR Studies of the Nitrogenase MoFe Protein under Turnover Conditions: Substrate-Inhibitor-Binding to and Metal-Ion Valencies of the FeMo-Cofactor / Lee, Hong-In, Department of Chemistry Education, Kyungpook National University, Daegu 702-701, Korea; Cameron, Linda M., Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803; Christiansen, Jason, Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061; Christie, Patricia D., Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139; Pollock, Robert C., Department of Chemistry, Northwestern University, Evanston, IL 60208; Song, Rutian, Department of Chemistry, Northwestern University, Evanston, IL 60208; Sørlie, Morten, Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803; Orme-Johnson, W. H., Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139; Dean, Dennis R., Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061; Hales, Brian J., Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803; Hoffman, Brian M., Department of Chemistry, Northwestern University, Evanston, IL 60208 / http://dx.doi.org/10.1021/bk-2003-0858.ch008 -- Variable Frequency Pulsed EPR Studies of Molybdenum Enzymes: Structure of Molybdenum Enzymes / Enemark, John H.; Astashkin, Andrei V.; Raitsimring, Arnold M. / http://dx.doi.org/10.1021/bk-2003-0858.ch009 -- Mn2+ Sites Investigated by Advanced EPR Techniques: In-Depth Study of Mn2+ Ion-Binding Sites in the Hammerhead Ribozyme / Vogt, Matthew; DeRose, Victoria J. / http://dx.doi.org/10.1021/bk-2003-0858.ch010 -- Structure and Dynamics of Paramagnetic Proteins by NMR / Kostic, Milka; Pochapsky, Thomas C. / http://dx.doi.org/10.1021/bk-2003-0858.ch011 -- An Approach to NMR Treatment of Structural Perturbations in Paramagnetic Proteins too Big for Solution Structure Determination / Nocek, Judith M., Department of Chemistry, NMR Facility, Northwestern University, 2145 North Sheridan Road, Evanston, IL 60208; Huang, Kai, Department of Structural Biology, NMR Facility, Northwestern University, 2145 North Sheridan Road, Evanston, IL 60208; Hoffman, Brian M., Department of Chemistry, NMR Facility, Northwestern University, 2145 North Sheridan Road, Evanston, IL 60208 / http://dx.doi.org/10.1021/bk-2003-0858.ch012 -- Proton NMR Characterization of Recombinant Ferric Heme Domains of the Oxygen Sensors FixL and Dos: Evidence for Protein Heterogeneity / Satterlee, James D.; Suquet, Christine M.; Savenkova, Marina I.; Lian, Chenyang / http://dx.doi.org/10.1021/bk-2003-0858.ch013.
NMR Investigation of the Iron-Sulfur Cluster Environment in the Hyperthermostable Ferredoxin from Pyrococcus furiosus / Calzolai, Luigi, Department of Chemistry, University of California, Davis, CA 95616, Current address: Institute for Molecular Biology and Biophysics, ETH-Honggerberger, HPK CH-8093, Zurich, Switzerland; Haarklau, Halvard, Department of Chemistry, University of California, Davis, CA 95616; Brereton, Philip S., Department of Biochemistry and Molecular Biology, Center for Metalloenzyme Studies, University of Georgia, B/22 Life Sciences Building, Green Street, Athens, GA 30602; Adams, Michael W. W., Department of Biochemistry and Molecular Biology, Center for Metalloenzyme Studies, University of Georgia, B/22 Life Sciences Building, Green Street, Athens, GA 30602; La Mar, Gerd N., Department of Chemistry, University of California, Davis, CA 95616 / http://dx.doi.org/10.1021/bk-2003-0858.ch014 -- Electronic Isomerism in Oxidized High-Potential Iron-Sulfur Proteins Revisited / Bertini, Ivano, Center of Magnetic Resonance, University of Florence, Via Luigi Sacconi 6, IT-50019, Florence, Italy; Capozzi, Francesco, Department of Food Science, University of Bologna, Via Ravennate 1020, IT-47023, Cesena (FC), Italy; Luchinat, Claudio, Center of Magnetic Resonance, University of Florence, Via Luigi Sacconi 6, IT-50019, Florence, Italy / http://dx.doi.org/10.1021/bk-2003-0858.ch015 -- Paramagnetic NMR of Electron Transfer Copper Proteins / Fernández, Claudio O., LANAIS-RMN, CONICET, University of Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina; Vila, Alejandro J., Instituto de Biología Molecular y Celular de Rosario (IBR), University of Rosario, Suipacha 531, 2000 Rosario, Argentina / http://dx.doi.org/10.1021/bk-2003-0858.ch016 -- Applications of Paramagnetic NMR Spectroscopy for Monitoring Transition Metal Complex Stoichiometry and Speciation / Crans, Debbie C., Department of Chemistry, Colorado State University, Fort Collins, CO 80523-1872; Yang, Luqin, Department of Chemistry, Colorado State University, Fort Collins, CO 80523-1872; Gaidamauskas, Ernestas, Department of Chemistry, Colorado State University, Fort Collins, CO 80523-1872; Khan, Raza, Department of Chemistry, Colorado State University, Fort Collins, CO 80523-1872; Jin, Wenzheng, Department of Chemistry, Colorado State University, Fort Collins, CO 80523-1872; Simonis, Ursula, Department of Chemistry and Biochemistry, San Francisco State University, 1600 Holloway Avenue, San Francisco, CA 94132-4163 / http://dx.doi.org/10.1021/bk-2003-0858.ch017 -- Variable-Temperature Variable-Field Magnetic Circular Dichroism Combined with Electron Paramagnetic Resonance: Polarizations of Electronic Transitions in Solution / Solomon, Edward I.; Davis, Mindy I.; Neese, Frank; Pau, Monita Y. M. / http://dx.doi.org/10.1021/bk-2003-0858.ch018 -- Magnetic Circular Dichroism Spectroscopy of Pyranopterin Molybdenum Enzymes / Kirk, Martin L. / http://dx.doi.org/10.1021/bk-2003-0858.ch019 -- X-ray Magnetic Circular Dichroism: A Primer for Chemists / Cramer, Stephen P. / http://dx.doi.org/10.1021/bk-2003-0858.ch020.
Summary Annotation Paramagnetic transition metal ions provide the opportunity for application of a wide variety of spectroscopic techniques. Although spectroscopic techniques are not as well known as conventional nuclear magnetic resonance (NMR), they provide detailed information centered on the active site itself. This book describes the application of paramagnetic resonance techniques to a number of important systems in metallobiochemistry. Simultaneously, this volume provides information on novel experimantal methods and theoretical approaches to understanding the structure and function of metalloenzymes and other metallobiomolecules. The specific techniques described include electron paramagnetic resonance (EPR) spectroscopy, and its derivative techniques, electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM). These latter two techniques directly probe the nuclear environment of the paramagnetic active site, without interference from magnetically active nuclei that are not involved in the active site. Magnetic circular dichroism (MCD), which links magnetic resonance and oprical spectrospoy, is also described. The application of MCD to problems in metallobiochemistry is growing rapidly, yet uhere are few sources that clearly describe this complex technique. This volume provides several approaches involving MCD. Finally, this book also includes a wide variety of biological systems including heme proteins, iron-sulfur proteins, molybdopterins, manganese proteins, and copper proteins, as well as non-protein biological molecules, such as ribozymes.
Other Author Telser, Joshua A., 1958-
American Chemical Society. Division of Inorganic Chemistry.
American Chemical Society. Meeting (223rd : 2002 : Orlando, Fla.)
Other Title Print version: Paramagnetic resonance of metallobiomolecules. Washington, D.C. : American Chemical Society, ©2003 0841238324