Autor: Heinz–Bernhard Kraatz, Nils Metzler–Nolte
Wydawca: Wiley
Dostępność: 3-6 tygodni
Cena: 394,80 zł
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ISBN13: |
9783527313051 |
ISBN10: |
3527313052 |
Autor: |
Heinz–Bernhard Kraatz, Nils Metzler–Nolte |
Oprawa: |
Paperback |
Rok Wydania: |
2006-06-16 |
Ilość stron: |
469 |
Wymiary: |
241x186 |
Tematy: |
PN |
Destined to set the standard, this book meets the need for a didactic textbook focusing on the role of model systems in bioinorganic chemistry. The first part features concepts in bioinorganic chemistry such as electron transfer, medicinal inorganic chemistry, bioorganometallics and metal DNA complexes, while the second part presents inorganic model chemistry on metallo–enzymes, organized by metal ion.
Experts in the pertinent fields provide a didactically well–organized background on relevant biological systems, as well as on their structural, functional and spectroscopic properties. All chapters are similarly structured, each one beginning with a timeline featuring the most important historical facts on the subject, followed by a table of the most significant enzymes. The authors also summarize key developments and open questions within the respective model systems.
This book is aimed at senior undergraduate and graduate students in chemistry, biochemistry, life science and related fields.
Spis treści:
Foreword.
Preface.
List of Contributors.
Abbreviations.
1 The Biodistribution of Metal Ions (Robert J. P. Williams).
1.1 Introduction.
1.2 Rates of Exchange.
1.3 The Limitations of Water as a Solvent.
1.4 Equilibrium: Values of Binding Constants.
1.5 Quantitative Metal Ion Equilibria: Donor Strength.
1.6 The Effect of Size and Charge of Metal Ions.
1.7 The Effect of Electron Affi nity.
1.8 Control over Ligand Concentration.
1.9 The Compartments of Organisms.
1.10 Transport.
1.11 The Irreversible Binding of Fe, Co, Ni, Mg, and Mo (W).
1.12 Vanadium, Molybdenum, and Tungsten.
1.13 Rates of Exchange.
1.14 Summary.
2 Medicinal Inorganic Chemistry (Katherine H. Thompson and Chris Orvig).
2.1 Introduction.
2.2 Key Developments.
2.3 Summary of Key Concepts.
2.4 Selected Current Research Directions.
2.5 Open
Questions.
3 The Chemical Toxicology of Metals and Metalloids (Graham N. George).
3.1 Introduction.
3.2 Arsenic.
3.3 Mercury.
3.4 Chromium.
3.5 The Promise of New Techniques.
4 Theoretical Modeling of Redox Processes in Enzymes and Biomimetic Systems (Arianna Bassan, Tomasz Borowski, Marcus Lundberg, and Per E. M. Siegbahn).
4.1 Introduction.
4.2 Computational Model.
4.3 Nonheme Iron Active Sites That Perform Alkane Hydroxylation and Olefin Oxidation.
4.4 Keto Acid–Dependent Dioxygenases and Their Synthetic Analogues.
4.5 Copper Complexes in Enzymes and Synthetic Systems.
4.6 Manganese Complexes That Oxidize Water to Dioxygen.
4.7 Conclusions.
5 Charge Transport in Biological Molecules (Yitao Long and Heinz–Bernhard Kraatz).
5.1 Introduction.
5.2 Electron Transfer in Proteins.
5.3 Electron Transfer in Peptides.
5.4 Charge Transfer in DNA.
5.5 Summary and Open Questions.
6 Bioorganometallic Chemistry (Nils Metzler–Nolte and Kay Severin).
6.1 Introduction.
6.2 Organometallic Complexes in Nature.
6.3 Synthetic Organometallic Complexes with Bioligands.
6.4 Organometallic Pharmaceuticals.
6.5 Analytical Bioorganometallic Chemistry.
6.6 Bioorganometallic Catalysis.
6.7 Conclusions and Outlook.
7 The Bioinorganic Side of Nucleic Acid Chemistry: Interactions with Metal Ions (Bernhard Lippert and Jens Müller).
7.1 Introduction: Nucleic Acids and Metals.
7.2 Modeling Metal–Nucleic Acid Interactions.
7.3 Take–Home Message.
7.4 Open Questions and Perspectives.
8 Nuclease and Peptidase Models (Srecko I. Kirin, Roland Krämer, and Nils Metzler–Nolte).
8.1 Introduction.
8.2 Mechanistic Considerations.
8.3 Substrates for Model Studies.
8.4 Peptidase Models.
8.5 Nuclease Models.
8.6 Applications.
9 Metalloporphyrins, Metalloporphy
rinoids, and Model Systems (Bernhard Kräutler and Bernhard Jaun).
9.1 Introduction: Biological Background.
9.2 Model Systems and Model Compounds to Understand Biological Function.
9.3 Summary of Key Concepts.
9.4 Open Questions and the Direction of Future Research.
10 Model Complexes for Vanadium–Containing Enzymes (Dieter Rehder).
10.1 Biological Background and Motivation.
10.2 Model Compounds.
10.3 Summary of Key Concepts.
10.4 Open Questions and the Direction of Future Research.
11 Model Complexes for Molybdenum– and Tungsten–Containing Enzymes (John H. Enemark and J. Jon A. Cooney).
11.1 Biological Background and Motivation.
11.1.1 Introduction 238
11.2 Model Compounds.
11.3 Summary.
11.4 Open Questions.
12 Structural and Functional Models for Oxygen–Activating Nonheme Iron Enzymes (Timothy A. Jackson and Lawrence Que, Jr.).
12.1 Biological Background and Motivation.
12.2 Dinuclear Iron Centers.
12.3 Diiron Models.
12.4 Monoiron Active Sites with a 2–His–1–Carboxylate Facial Triad Motif.
12.5 Monoiron Models.
12.6 Summary of Key Concepts.
12.7 Open Questions and the Direction of Future Research.
13 Model Chemistry of the Iron–Sulfur Protein Active Sites (George A. Koutsantonis).
13.1 Introduction.
13.2 Basic Iron and Sulfur Chemistry.
13.3 Common Iron–Sulfur Geometries.
13.4 Required Protein and Peptide Coordination Environments.
13.5 Syntheses of Model Compounds.
13.6 Properties of Analogues and Their Relation to Protein–Bound Clusters.
13.7 Conclusions.
14 Model Complexes of Ni–Containing Enzymes (Todd C. Harrop and Pradip K. Mascharak).
14.1 Introduction.
14.2 Urease.
14.3 NiFe Hydrogenase.
14.4 Carbon Monoxide Dehydrogenase/Acetyl Coenzyme A Synthase (CODH/ACS).
14.5 Conclusions.
15 Hyd
rogenases and Model Complexes (Robert H. Morris).
15.1 Introduction.
15.2 What are Hydrogenases?
15.3 Nickel–Iron (NiFe–Hase) and Nickel–Iron–Selenium (NiFeSe–Hase) Hydrogenases.
15.4 Iron–Iron Hydrogenases.
15.5 Similarities and Differences between NiFe–Hase and FeFe–Hase.
15.6 Synthetic Complexes that Model Hydrogenases.
15.7 Conclusions.
15.8 Open Questions and the Direction of Future Research.
16 Model Complexes for Copper–Containing Enzymes (Yunho Lee and Kenneth D. Karlin).
16.1 Introduction.
16.2 Biological Background: Copper Proteins and Motivation for Biomimetic Studies.
16.3 Model Compounds.
16.4 Summary of Key Concepts.
16.5 Open Questions and Directions for Future Research.
17 Model Complexes for Zinc–Containing Enzymes (Nicolai Burzlaff).
17.1 Introduction.
17.2 Mononuclear Zinc Enzymes and Models.
17.3 Dinuclear Zinc Enzymes and Models.
17.4 Conclusions.
Subject Index.
Nota biograficzna:
Heinz–Bernhard Kraatz obtained his Ph.D. from the University of Calgary in 1993 (inorganic chemistry, with P. M. Boorman). After a shorter stay at the University of Maryland, he spent two years at the Weizmann Institute as a Minerva postdoctoral fellow (1994–1995). He was a Research associate at the National Research Council of Canada (1996–1997). In 1998 he was appointed to the University of Saskatchewan, where was Associate Professor since 2001 and became full Professor in 2006. HBK is the Canada Reseach Chair in Biomaterials. He received several awards and was the organizer of meetings in bioinorganic chemistry and electrochemistry in Canada. Research in his group focusses on the design of peptides and surface–supported peptide assemblies modified by inorganic and organometallic moieties to study electron transfer and to develop new biosensors.
Nils
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