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The Resource Metals in biology : applications of high-resolution EPR to metalloenzymes, Graeme Hanson, Lawrence Berliner, editors, (electronic resource)
Metals in biology : applications of high-resolution EPR to metalloenzymes, Graeme Hanson, Lawrence Berliner, editors, (electronic resource)
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The item Metals in biology : applications of high-resolution EPR to metalloenzymes, Graeme Hanson, Lawrence Berliner, editors, (electronic resource) represents a specific, individual, material embodiment of a distinct intellectual or artistic creation found in University of Oklahoma Libraries.This item is available to borrow from all library branches.
Resource Information
The item Metals in biology : applications of high-resolution EPR to metalloenzymes, Graeme Hanson, Lawrence Berliner, editors, (electronic resource) represents a specific, individual, material embodiment of a distinct intellectual or artistic creation found in University of Oklahoma Libraries.
This item is available to borrow from all library branches.
- Summary
- 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
- Language
-
- eng
- eng
- Extent
- 1 online resource (426 p.)
- Note
- Description based upon print version of record
- 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
- Isbn
- 9781282831117
- Label
- Metals in biology : applications of high-resolution EPR to metalloenzymes
- Title
- Metals in biology
- Title remainder
- applications of high-resolution EPR to metalloenzymes
- Statement of responsibility
- Graeme Hanson, Lawrence Berliner, editors
- Language
-
- eng
- eng
- Summary
- 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
- Cataloging source
- MiAaPQ
- Dewey number
- 538.364
- Illustrations
- illustrations
- Index
- index present
- Language note
- English
- LC call number
- QH324.9.E36
- LC item number
- M48 2010
- Literary form
- non fiction
- Nature of contents
-
- dictionaries
- bibliography
- http://library.link/vocab/relatedWorkOrContributorName
-
- Hanson, Graeme Richard
- Berliner, Lawrence J
- Series statement
- Biological magnetic resonance
- Series volume
- v. 29
- http://library.link/vocab/subjectName
-
- Electron paramagnetic resonance
- Metalloenzymes
- Label
- Metals in biology : applications of high-resolution EPR to metalloenzymes, Graeme Hanson, Lawrence Berliner, editors, (electronic resource)
- Note
- Description based upon print version of record
- Bibliography note
- Includes bibliographical references and index
- Carrier category
- online resource
- Carrier category code
-
- cr
- Content category
- text
- Content type code
-
- txt
- 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
- Dimensions
- unknown
- Extent
- 1 online resource (426 p.)
- Form of item
- online
- Isbn
- 9781282831117
- Media category
- computer
- Media type code
-
- c
- Other control number
- 10.1007/978-1-4419-1139-1
- Specific material designation
- remote
- System control number
-
- (CKB)2670000000017233
- (EBL)690932
- (OCoLC)663096169
- (SSID)ssj0000398768
- (PQKBManifestationID)11273148
- (PQKBTitleCode)TC0000398768
- (PQKBWorkID)10375297
- (PQKB)11261036
- (DE-He213)978-1-4419-1139-1
- (MiAaPQ)EBC690932
- (EXLCZ)992670000000017233
- Label
- Metals in biology : applications of high-resolution EPR to metalloenzymes, Graeme Hanson, Lawrence Berliner, editors, (electronic resource)
- Note
- Description based upon print version of record
- Bibliography note
- Includes bibliographical references and index
- Carrier category
- online resource
- Carrier category code
-
- cr
- Content category
- text
- Content type code
-
- txt
- 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
- Dimensions
- unknown
- Extent
- 1 online resource (426 p.)
- Form of item
- online
- Isbn
- 9781282831117
- Media category
- computer
- Media type code
-
- c
- Other control number
- 10.1007/978-1-4419-1139-1
- Specific material designation
- remote
- System control number
-
- (CKB)2670000000017233
- (EBL)690932
- (OCoLC)663096169
- (SSID)ssj0000398768
- (PQKBManifestationID)11273148
- (PQKBTitleCode)TC0000398768
- (PQKBWorkID)10375297
- (PQKB)11261036
- (DE-He213)978-1-4419-1139-1
- (MiAaPQ)EBC690932
- (EXLCZ)992670000000017233
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<div class="citation" vocab="http://schema.org/"><i class="fa fa-external-link-square fa-fw"></i> Data from <span resource="http://link.libraries.ou.edu/portal/Metals-in-biology--applications-of/opr6AKdoZS8/" typeof="Book http://bibfra.me/vocab/lite/Item"><span property="name http://bibfra.me/vocab/lite/label"><a href="http://link.libraries.ou.edu/portal/Metals-in-biology--applications-of/opr6AKdoZS8/">Metals in biology : applications of high-resolution EPR to metalloenzymes, Graeme Hanson, Lawrence Berliner, editors, (electronic resource)</a></span> - <span property="potentialAction" typeOf="OrganizeAction"><span property="agent" typeof="LibrarySystem http://library.link/vocab/LibrarySystem" resource="http://link.libraries.ou.edu/"><span property="name http://bibfra.me/vocab/lite/label"><a property="url" href="http://link.libraries.ou.edu/">University of Oklahoma Libraries</a></span></span></span></span></div>
