rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Metals in Biology
    sub title: Applications of High-Resolution EPR to Metalloenzymes
  name:
    name part: Hanson, Graeme.
    role:
      role term: editor.
  name:
    name part: Berliner, Lawrence.
    role:
      role term: editor.
  name:
    name part: SpringerLink (Online service)
  type of resource: text
  origin info:
    place:
      place term: xxu
    date issued: 2010
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    form: electronic resource
    reformatting quality: access
    form: remote
    extent: XIX, 419 p. online resource.
  abstract: 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 …
  table of contents: IRON–SULFUR-CONTAINING PROTEINS -- Electron Magnetic Resonance of Iron#x2013;Sulfur Proteins in Electron-Transfer Chains: Resolving Complexity -- Catalysis and Gene Regulation -- Iron#x2013;Sulfur Clusters in #x201C;Radical SAM#x201D; Enzymes: Spectroscopy and Coordination -- MONONUCLEAR MOLYBDENUM ENZYMES -- EPR Studies of Xanthine Oxidoreductase and Other Molybdenum-Containing Hydroxylases -- High-Resolution EPR Spectroscopy of Mo Enzymes. Sulfite Oxidases: Structural and Functional Implications -- Dimethylsulfoxide (DMSO) Reductase, a Member of the DMSO Reductase Family of Molybdenum Enzymes -- MANGANESE-CONTAINING ENZYMES -- The Manganese-Calcium Cluster of the Oxygen-Evolving System: Synthetic Models, EPR Studies, and Electronic Structure Calculations -- Manganese Metalloproteins -- NOVEL METALLOENZYMES AND METALLOPROTEINS -- EPR of Cobalt-Substituted Zinc Enzymes -- Hyperfine and Quadrupolar Interactions in Vanadyl Proteins and Model Complexes: Theory and Experiment.
  note: edited by Graeme Hanson, Lawrence Berliner.
  subject:
    topic: Medicine
  subject:
    topic: Biomedical engineering
  subject:
    topic: Materials science
  subject:
    topic: Biomedicine
  subject:
    topic: Biomedicine general
  subject:
    topic: Materials Science, general
  subject:
    topic: Biomedical Engineering
  classification: R-RZ
  classification: 610
  related item:
    title info:
      title: Springer eBooks
  related item:
    title info:
      title: Biological Magnetic Resonance, 29
  identifier: 9781441911391
  identifier: http://dx.doi.org/10.1007/978-1-4419-1139-1
  record info:
    record creation date: 100715
    record change date: 20151204153017.0
    record identifier: 978-1-4419-1139-1