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Metals in Biology (Record no. 17203)

000 -LEADER
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003 - CONTROL NUMBER IDENTIFIER
control field OSt
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20140310150232.0
007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION
fixed length control field cr nn 008mamaa
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 100715s2010 xxu| s |||| 0|eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9781441911391
978-1-4419-1139-1
050 #4 - LIBRARY OF CONGRESS CALL NUMBER
Classification number R-RZ
082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 610
Edition number 23
264 #1 -
-- New York, NY :
-- Springer New York,
-- 2010.
912 ## -
-- ZDB-2-SBL
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Hanson, Graeme.
Relator term editor.
245 10 - IMMEDIATE SOURCE OF ACQUISITION NOTE
Title Metals in Biology
Medium [electronic resource] :
Remainder of title Applications of High-Resolution EPR to Metalloenzymes /
Statement of responsibility, etc edited by Graeme Hanson, Lawrence Berliner.
300 ## - PHYSICAL DESCRIPTION
Extent XIX, 419p.
Other physical details online resource.
440 1# - SERIES STATEMENT/ADDED ENTRY--TITLE
Title Biological Magnetic Resonance,
International Standard Serial Number 0192-6020 ;
Volume number/sequential designation 29
505 0# - FORMATTED CONTENTS NOTE
Formatted contents note IRON–SULFUR-CONTAINING PROTEINS -- Electron Magnetic Resonance of Iron–Sulfur Proteins in Electron-Transfer Chains: Resolving Complexity -- Catalysis and Gene Regulation -- Iron–Sulfur Clusters in “Radical SAM” 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.
520 ## - SUMMARY, ETC.
Summary, etc 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
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Medicine.
Topical term or geographic name as entry element Materials.
Topical term or geographic name as entry element Biomedicine.
Topical term or geographic name as entry element Biomedicine general.
Topical term or geographic name as entry element Materials Science, general.
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Berliner, Lawrence.
Relator term editor.
710 2# - ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element SpringerLink (Online service)
773 0# - HOST ITEM ENTRY
Title Springer eBooks
776 08 - ADDITIONAL PHYSICAL FORM ENTRY
Display text Printed edition:
International Standard Book Number 9781441911384
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier http://dx.doi.org/10.1007/978-1-4419-1139-1
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme
Item type E-Book
Copies
Price effective from Permanent location Date last seen Not for loan Date acquired Source of classification or shelving scheme Koha item type Damaged status Lost status Withdrawn status Current location Full call number
2014-04-03AUM Main Library2014-04-03 2014-04-03 E-Book   AUM Main Library610
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