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

Author(s): John R. Pilbrow (auth.), Graeme Hanson, Lawrence Berliner (eds.)
Series: Biological Magnetic Resonance 29
Edition: 1
Publisher: Springer-Verlag New York
Year: 2010

Language: English
Pages: 419
Tags: Biomedicine general; Materials Science, general

Front Matter....Pages 1-17
Introduction....Pages 1-7
Front Matter....Pages 9-9
Electron Magnetic Resonance of Iron–Sulfur Proteins in Electron-Transfer Chains: Resolving Complexity....Pages 11-44
Catalysis and Gene Regulation....Pages 45-51
Iron–Sulfur Clusters in “Radical SAM” Enzymes: Spectroscopy and Coordination....Pages 53-82
Front Matter....Pages 83-89
EPR Studies of Xanthine Oxidoreductase and Other Molybdenum-Containing Hydroxylases....Pages 91-120
High-Resolution EPR Spectroscopy of Mo Enzymes. Sulfite Oxidases: Structural and Functional Implications....Pages 121-168
Dimethylsulfoxide (DMSO) Reductase, a Member of the DMSO Reductase Family of Molybdenum Enzymes....Pages 169-199
Front Matter....Pages 201-201
The Manganese-Calcium Cluster of the Oxygen-Evolving System: Synthetic Models, EPR Studies, and Electronic Structure Calculations....Pages 203-271
Manganese Metalloproteins....Pages 273-341
Front Matter....Pages 343-343
EPR of Cobalt-Substituted Zinc Enzymes....Pages 345-370
Hyperfine and Quadrupolar Interactions in Vanadyl Proteins and Model Complexes: Theory and Experiment....Pages 371-409
Back Matter....Pages 1-9