Metals In Biology: Applications Of High-resolution Epr To Metalloenzymes

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Metals in Biology Applications of High Resolution EPR to Metalloenzymes

Prof. Graeme R. Hanson, University of Queensland and Prof. Lawrence J. Berliner, University of Denver

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. The following chapters, written by experts in their fields, include:

  • An Introduction: John Pilbrow
  • Electron Magnetic Resonance of Iron-sulfur Proteins in Electron Transfer Chains - Resolving Complexity: Richard Cammack, Fraser MacMillan
  • Catalysis and Gene Regulation: Helmut Beinert
  • Iron Sulfur Clusters in Radical SAM Enzymes: Spectroscopy and Coordination: Serge Gambarelli, Etienne Mulliez, Marc Fontecave
  • EPR Studies of Xanthine Oxidoreductase and Other Molybdenum-containing Hydroxylases: Russ Hille
  • High Resolution EPR Spectroscopy of Mo-enzymes. Sulfite Oxidases: Structural and Functional Implications: John Enemark, Andrei Astashkin, Arnold Raitsimring
  • Dimethylsulfoxide (DMSO) Reductase, a Member of the DMSO Reductase Family of Molybdenum Enzymes: Graeme Hanson, Ian Lane
  • The Manganese-Calcium Cluster of the Oxygen Evolving System: Synthetic Models, EPR Studies, and Electronic Structure Calculations: Marcin Brynda, David Britt
  • Binuclear Manganese-dependent enzymes: Sarah Smith, Kieran Hadler, Gerhard Schenk, Graeme Hanson, Nataša Mitic
  • EPR of Cobalt-Substituted Zinc Enzymes: Brian Bennett
  • Hyperfine and Quadrupolar Interactions in Vanadyl Protein and Model Complexes. Theory and Experiment: Sarah Larsen, Dennis Chasteen


E-Book Content

Biological Magnetic Resonance Volume 29 For further volumes: http://www.springer.com/series/5693 A Continuation Order Plan is available for this series. A continuation order will bring delivery of each new volume immediately upon publication. Volumes are billed only upon actual shipment. For further information please contact the publisher. Graeme Hanson • Lawrence Berliner Editors Metals in Biology Applications of High-Resolution EPR to Metalloenzymes Volume 29 Editors Graeme Hanson Centre for Magnetic Resonance The University of Queensland St. Lucia, QLD 4072 Australia [email protected] Lawrence Berliner University of Denver 2190 E. Iliff Avenue, Room 202 Denver, CO 80208-0001 USA [email protected] ISSN 0192-6020 ISBN 978-1-4419-1138-4 e-ISBN 978-1-4419-1139-1 DOI 10.1007/978-1-4419-1139-1 Springer New York Dordrecht Heidelberg London Library of Congress Control Number: 2009939429 © Springer Science+Business Media
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