Concepts and models in bioinorganic chemistry

Başlık:

Yazar:

Kraatz, Heinz-Bernhard.

ISBN:

9783527313051

Yayım Bilgisi:

Weinheim : Wiley-VCH, c2006.

Fiziksel Tanım:

xxvi, 443 s. : şkl. ; 24 cm.

Contents:

The biodistribution of metal ions / Medicinal inorganic chemistry / The chemical toxicology of metals and metalloids / Theoretical modeling of redox processes in enzymes and biomimetic systems / Charge transport in biological molecules / Bioorganometallic chemistry / The bioinorganic side of nucleic acid chemistry: interactions with metal ions / Nuclease and peptidase models / Metalloporphyrins, metalloporphyrinoids, and model systems / Model complexes for vanadium-containing enzymes / Model complexes for molybdenum- and tungsten-containing enzymes / Structural and functional models for oxygen-activating nonheme iron enzymes / Model chemistry of the iron-sulfur protein active sites / Model complexes of Ni-containing enzymes / Hydrogenases and model complexes / Model complexes for copper-containing enzymes / Model complexes for zinc-containing enzymes

Konu Terimleri:

Biyoinorganik kimya.

Bioinorganic chemistry.

Added Author:

Kraatz, Heinz-Bernhard.

Metzler-Nolte, Nils.

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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.

Author Notes

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 he 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 Metzler-Nolte (ne Metzler) obtained his Ph.D. from the University of Munich in 1994 (Organoboron chemistry, with H. Noth). After a postdoctoral year with M. L. H. Green in Oxford, he started independent research at the Max-Planck-Institut fur Strahlenchemie (now MPI for Bioinorganic Chemistry). He obtained his Habilitation at the University of Bochum in May 2000 and was soonafter appointed Professor for bioinorganic chemistry at the University of Heidelberg. In 2006, he accepted a Chair for Inorganic Chemistry at the University of Bochum. His work has been recognized by several awards and he has organized national and international conferences in bioorganometallic chemistry. His research interest is in bioorganometallic chemistry and functional bioconjugates with transition metals, including aspects of medicinal inorganic chemistry.

Reviews (1)

Choice Review

Concepts and Models in Bioinorganic Chemistry is the latest in a small group of course resources centered around this emerging subfield of chemistry, one of only two published in the past ten years. Unlike its contemporary Bioinorganic Chemistry: A Short Course, by Rosette M. Roat-Malone (CH, May'03, 40-5232), Concepts and Models is designed for the more advanced student or researcher in this field. It is organized into 17 chapters, each of which treats a separate topic in bioinorganic chemistry. With the exception of the first chapter, each additional chapter functions as a review of the current state of knowledge for each subtopic. Individual chapters are written by separate authors or teams of coauthors, respected researchers in that specific subtopic. This book will be an essential resource for any graduate student or researcher in the field. Not appropriate for undergraduates. ^BSumming Up: Highly recommended. Graduate students through professionals. R. M. Granger II Sweet Briar College

Robert J. P. WilliamsKatherine H. Thompson and Chris OrvigGraham N. GeorgeArianna Bassan and Tomasz Borowski and Marcus Lundberg and Per E. M. SiegbahnYitao Long and Heinz-Bernhard KraatzNils Metzler-Nolte and Kay SeverinBernhardt Lippert and Jens MullerSrecko I. Kirin and Roland Kramer and Nils Metzler-NolteBernhard Krautler and Bernhard JaunDieter RehderJohn H. Enemark and J. Jon A. CooneyTimothy A. Jackson and Lawrence Que, Jr.George A. KoutsantonisTodd C. Harrop and Pradip K. MascharakRobert H. MorrisYunho Lee and Kenneth D. KarlinNicolai Burzlaff

Foreword	p. V
Preface	p. VII
List of Contributors	p. XIX
Abbreviations	p. XXIII
1 The Biodistribution of Metal Ions	p. 1
1.1 Introduction	p. 2
1.2 Rates of Exchange	p. 5
1.3 The Limitations of Water as a Solvent	p. 5
1.4 Equilibrium: Values of Binding Constants	p. 7
1.5 Quantitative Metal Ion Equilibria: Donor Strength	p. 7
1.6 The Effect of Size and Charge of Metal Ions	p. 8
1.7 The Effect of Electron Affinity	p. 11
1.8 Control over Ligand Concentration	p. 14
1.9 The Compartments of Organisms	p. 16
1.10 Transport	p. 18
1.11 The Irreversible Binding of Fe, Co, Ni, Mg, and Mo (W)	p. 19
1.12 Vanadium, Molybdenum, and Tungsten	p. 20
1.13 Rates of Exchange	p. 21
1.14 Summary	p. 22
References	p. 23
2 Medicinal Inorganic Chemistry	p. 25
2.1 Introduction	p. 26
2.2 Key Developments	p. 27
2.2.1 Therapeutic Agents	p. 27
2.2.1.1 Arsphenamine: The First Comprehensive Structure-Activity Relationship	p. 28
2.2.1.2 Lithium in Psychiatry: The Dose-Response Relationship	p. 29
2.2.1.3 Cisplatin: Targeted Toxicity	p. 31
2.2.1.4 The Discovery of Essential Trace Elements	p. 32
2.2.1.5 Treatment of Copper- and Iron-Overload Disorders: Metal Ions as Targets	p. 33
2.2.1.6 Radiopharmaceuticals: Utilizing the Nuclear Properties of Metal Ions	p. 34
2.2.2 Diagnostic Agents	p. 35
2.2.2.1 [superscript 99m] Tc-Labeled Diagnostic Agents	p. 36
2.2.2.2 Targeted Myocardial Imaging with [superscript 99m] Tc-Sestamibi	p. 36
2.2.2.3 [superscript 67]Ga-Citrate Scintigraphy: Computed Tomography	p. 37
2.2.2.4 [superscript 111]In-DTPA-Octreotide-Peptide Binding for Improved Tissue Targeting	p. 37
2.2.2.5 Gadolinium-based MRI Contrast Enhancement	p. 38
2.3 Summary of Key Concepts	p. 39
2.4 Selected Current Research Directions	p. 39
2.4.1 Therapeutic Agents	p. 39
2.4.1.1 Vanadyl Insulin Mimetic Agents: Anticipating Biomolecular Interaction	p. 39
2.4.1.2 Multifunctional Antimalarial Metallopharmaceuticals	p. 40
2.4.1.3 Using Oxidation State to Advantage: Pt(IV) Compounds	p. 41
2.4.2 Diagnostic Agents	p. 41
2.5 Open Questions	p. 42
References	p. 44
3 The Chemical Toxicology of Metals and Metalloids	p. 47
3.1 Introduction	p. 48
3.2 Arsenic	p. 48
3.2.1 Dietary Sources of Arsenic	p. 51
3.2.2 Arsenic-Selenium Antagonism: Two Wrongs That Do Make a Right!	p. 52
3.3 Mercury	p. 52
3.3.1 Mercury in Food	p. 55
3.3.2 Mercury-Selenium Antagonism and Synergism	p. 56
3.3.3 Mercury Chelation Therapy	p. 57
3.4 Chromium	p. 58
3.5 The Promise of New Techniques	p. 58
References	p. 59
4 Theoretical Modeling of Redox Processes in Enzymes and Biomimetic Systems	p. 63
4.1 Introduction	p. 64
4.2 Computational Model	p. 66
4.3 Nonheme Iron Active Sites That Perform Alkane Hydroxylation and Olefin Oxidation	p. 68
4.4 Keto Acid-Dependent Dioxygenases and Their Synthetic Analogues	p. 72
4.5 Copper Complexes in Enzymes and Synthetic Systems	p. 76
4.5.1 Enzymes with Copper Dimer Complexes	p. 76
4.5.2 Enzymes with Copper Monomer Complexes	p. 80
4.6 Manganese Complexes That Oxidize Water to Dioxygen	p. 81
4.6.1 The Electronic Structure of the Highly Oxidized State	p. 84
4.6.2 The O-O Bond-Formation Reaction	p. 86
4.7 Conclusions	p. 88
References	p. 88
5 Charge Transport in Biological Molecules	p. 93
5.1 Introduction	p. 94
5.1.1 A Brief History of Biological Electron Transfer	p. 95
5.1.2 Theoretical Considerations	p. 96
5.2 Electron Transfer in Proteins	p. 98
5.2.1 Studies Involving Metal-labeled Proteins	p. 99
5.2.1.1 Redox Properties	p. 100
5.2.1.2 Studies Involving Azurin	p. 100
5.3 Electron Transfer in Peptides	p. 103
5.4 Charge Transfer in DNA	p. 107
5.4.1 Fundamental Properties	p. 107
5.4.2 Molecular Diagnostics	p. 107
5.4.2.1 Sequence Detection	p. 107
5.4.2.2 Protein-DNA Interactions	p. 109
5.5 Summary and Open Questions	p. 110
References	p. 111
6 Bioorganometallic Chemistry	p. 113
6.1 Introduction	p. 115
6.2 Organometallic Complexes in Nature	p. 116
6.3 Synthetic Organometallic Complexes with Bioligands	p. 119
6.4 Organometallic Pharmaceuticals	p. 123
6.5 Analytical Bioorganometallic Chemistry	p. 125
6.6 Bioorganometallic Catalysis	p. 130
6.7 Conclusions and Outlook	p. 133
References	p. 134
7 The Bioinorganic Side of Nucleic Acid Chemistry: Interactions with Metal Ions	p. 137
7.1 Introduction: Nucleic Acids and Metals	p. 138
7.2 Modeling Metal-Nucleic Acid Interactions	p. 142
7.2.1 Selected "Classical" Aspects	p. 142
7.2.1.1 Metal-Binding Patterns	p. 142
7.2.1.2 Metals at Close Distance	p. 144
7.2.1.3 DNA Distortion by GG Adduct	p. 146
7.2.1.4 Pt Binding and NMR	p. 147
7.2.1.5 Subtle Consequences of Metal Coordination	p. 148
7.2.1.5.1 Effect of Metal Coordination on H Bonding	p. 148
7.2.1.5.2 Nucleobase Acidification	p. 148
7.2.1.5.3 Metals and Nucleobase Tautomerism	p. 149
7.2.1.6 Irreversible Nucleobase Modifications	p. 150
7.2.2 More Recent Developments	p. 151
7.2.2.1 Molecular Squares	p. 151
7.2.2.2 M-DNA	p. 152
7.2.2.3 Metal-Containing Antisense and Antigene Reagents	p. 153
7.2.2.4 Others	p. 154
7.3 Take-Home Message	p. 154
7.4 Open Questions and Perspectives	p. 155
References	p. 156
8 Nuclease and Peptidase Models	p. 159
8.1 Introduction	p. 159
8.2 Mechanistic Considerations	p. 161
8.3 Substrates for Model Studies	p. 163
8.4 Peptidase Models	p. 166
8.5 Nuclease Models	p. 167
8.5.1 Simple Mononuclear Metal Complexes	p. 167
8.5.2 Dinuclear Metal Complexes	p. 168
8.5.3 Metal-Functional Group Cooperation	p. 170
8.6 Applications	p. 172
References	p. 173
9 Metalloporphyrins, Metalloporphyrinoids, and Model Systems	p. 177
9.1 Introduction: Biological Background	p. 278
9.2 Model Systems and Model Compounds to Understand Biological Function	p. 182
9.2.1 Iron Porphyrins: Hemes in Biological Electron Transfer, Oxygen Transport and Activation	p. 188
9.2.1.1 Heme Proteins in Electron Transfer	p. 188
9.2.1.2 Heme Proteins in the Transport and Activation of Small Molecules	p. 189
9.2.2 Nickel Porphinoids: Coenzyme F430 in Biological Methane Formation	p. 193
9.2.2.1 The Redox Chemistry of Coenzyme F430 and its Derivatives	p. 194
9.2.2.2 Structure-Reactivity Relationships for Nickel Porphinoids	p. 195
9.2.2.3 Probing the Reactivity of Ni(I)F430M	p. 197
9.2.2.4 Synthetic Complexes as Models for Coenzyme F430	p. 199
9.2.3 Cobalt Corrinoids: Biological Organometallic Transformations	p. 199
9.2.4 Organometallic B[subscript 12] Derivatives and their Organometallic Reactivities	p. 204
9.3 Summary of Key Concepts	p. 207
9.4 Open Questions and the Direction of Future Research	p. 209
References	p. 209
10 Model Complexes for Vanadium-Containing Enzymes	p. 213
10.1 Biological Background and Motivation	p. 214
10.1.1 General Aspects of Vanadium Chemistry Related to Biological Functions	p. 214
10.1.2 Vanadium-Dependent Enzymes	p. 216
10.1.2.1 Haloperoxidases and Vanadate in Phosphoryl Transfer Enzymes	p. 216
10.1.2.2 Vanadium-Nitrogenase	p. 221
10.2 Model Compounds	p. 222
10.2.1 Models of Vanadate-Dependent Haloperoxidases	p. 222
10.2.2 Models of Vanadium-Nitrogenase	p. 227
10.3 Summary of Key Concepts	p. 229
10.4 Open Questions and the Direction of Future Research	p. 230
References	p. 232
11 Model Complexes for Molybdenum- and Tungsten-Containing Enzymes	p. 237
11.1 Biological Background and Motivation	p. 238
11.1.1 Introduction	p. 238
11.1.2 Enzyme Active Sites	p. 239
11.1.2.1 Structure	p. 239
11.1.2.2 Spectroscopy	p. 240
11.1.2.3 Reactivity	p. 241
11.1.3 Questions to be Answered by Model Compounds	p. 243
11.2 Model Compounds	p. 244
11.2.1 Background	p. 244
11.2.2 Stabilization of Mononuclear Oxo-Molybdenum Centers	p. 244
11.2.3 Electronic Contributions of Thiolate Ligands	p. 247
11.2.4 Towards Accurate Structural Models	p. 249
11.2.5 Reactivity and Spectroscopic Studies of {{MoS[subscript 4]}} Centers	p. 250
11.2.6 Computational Models of the XO Family	p. 251
11.3 Summary	p. 251
11.4 Open Questions	p. 252
References	p. 255
12 Structural and Functional Models for Oxygen-Activating Nonheme Iron Enzymes	p. 259
12.1 Biological Background and Motivation	p. 260
12.2 Dinuclear Iron Centers	p. 263
12.3 Diiron Models	p. 266
12.3.1 Structural Models	p. 266
12.3.2 Reactivity with O[subscript 2]	p. 268
12.3.3 Oxodiiron Intermediates	p. 270
12.4 Monoiron Active Sites with a 2-His-1-Carboxylate Facial Triad Motif	p. 272
12.4.1 [alpha]-Keto-acid-Dependent Enzymes	p. 272
12.4.2 Rieske Dioxygenases	p. 274
12.5 Monoiron Models	p. 275
12.5.1 Functional Models	p. 275
12.5.1.1 [alpha]KA-Dependent Enzymes	p. 275
12.5.1.2 Rieske Dioxygenases	p. 277
12.5.2 Oxoiron(IV) Intermediates	p. 280
12.6 Summary of Key Concepts	p. 282
12.7 Open Questions and the Direction of Future Research	p. 283
References	p. 283
13 Model Chemistry of the Iron-Sulfur Protein Active Sites	p. 287
13.1 Introduction	p. 288
13.2 Basic Iron and Sulfur Chemistry	p. 290
13.3 Common Iron-Sulfur Geometries	p. 290
13.4 Required Protein and Peptide Coordination Environments	p. 294
13.5 Syntheses of Model Compounds	p. 294
13.5.1 Mononuclear Rubredoxin Models [Fe-4S]	p. 294
13.5.2 Binuclear Ferredoxin Models [2Fe-2S]	p. 295
13.5.3 Trinuclear Analogues [3Fe-4S]	p. 296
13.5.3.1 Linear Analogues [3Fe-4S]	p. 296
13.5.3.2 Cubane-Derived Analogues [3Fe-4S]	p. 296
13.5.3.3 Tetranuclear Cubane Analogues [4Fe-4S]	p. 297
13.5.4 Non-Homoleptic Clusters [4Fe-4S]	p. 298
13.5.5 Models of Nitrogenase Clusters	p. 298
13.5.5.1 FeMoco Analogues	p. 300
13.5.5.2 P-Cluster Analogues	p. 301
13.6 Properties of Analogues and Their Relation to Protein-Bound Clusters	p. 302
13.6.1 Electrochemistry of Model Compounds	p. 303
13.6.2 Oxidation States and Mossbauer Studies	p. 303
References	p. 304
13.7 Conclusions	p. 304
14 Model Complexes of Ni-Containing Enzymes	p. 309
14.1 Introduction	p. 310
14.2 Urease	p. 310
14.2.1 The Enzyme	p. 310
14.2.2 Models	p. 312
14.3 NiFe Hydrogenase	p. 316
14.3.1 The Enzyme	p. 316
14.3.2 Models	p. 318
14.4 Carbon Monoxide Dehydrogenase/Acetyl Coenzyme A Synthase (CODH/ACS)	p. 320
14.4.1 The Enzyme	p. 320
14.4.2 Models	p. 322
14.5 Conclusions	p. 326
References	p. 327
15 Hydrogenases and Model Complexes	p. 331
15.1 Introduction	p. 332
15.2 What are Hydrogenases?	p. 332
15.3 Nickel-Iron (NiFe-Hase) and Nickel-Iron-Selenium (NiFeSe-Hase) Hydrogenases	p. 335
15.4 Iron-Iron Hydrogenases	p. 338
15.5 Similarities and Differences between NiFe-Hase and FeFe-Hase	p. 341
15.6 Synthetic Complexes that Model Hydrogenases	p. 342
15.6.1 Models of NiFe-Hase Active-Sites	p. 343
15.6.1.1 Ni Chemistry	p. 343
15.6.1.2 Hydride and Dihydrogen Chemistry and Electrocatalysis	p. 347
15.6.1.3 Iron Cyanide, Carbonyl Chemistry	p. 349
15.6.1.4 NiFe Bimetallic Model Complexes	p. 352
15.6.2 FeFe-Hase Models	p. 353
15.7 Conclusions	p. 358
15.8 Open Questions and the Direction of Future Research	p. 358
References	p. 359
16 Model Complexes for Copper-Containing Enzymes	p. 363
16.1 Introduction	p. 364
16.2 Biological Background: Copper Proteins and Motivation for Biomimetic Studies	p. 365
16.2.1 Copper Ion Properties and Biological Ligands	p. 365
16.2.2 Electron-Transfer Proteins	p. 368
16.2.2.1 Blue Copper Proteins	p. 368
16.2.2.2 Purple Cu[subscript A] Centers	p. 369
16.2.3 Dioxygen-Processing Proteins	p. 369
16.2.3.1 Dicopper Sites in Hemocyanin (Hc), Tyrosinase and CO	p. 370
16.2.3.2 Other Oxygenases	p. 371
16.2.3.3 Oxidases	p. 373
16.3 Model Compounds	p. 377
16.3.1 The Synthetic Model Approach for Copper and Cu[superscript 1]/O[subscript 2] Chemistry	p. 377
16.3.2 Dicopper O[subscript 2] Chemistry; Models for Cu[subscript 2]O[subscript 2] Proteins	p. 379
16.3.2.1 Side-on Peroxo Core	p. 379
16.3.2.2 End-on Peroxo Core	p. 380
16.3.2.3 Bis([mu]-oxo) Core	p. 381
16.3.2.4 Model for Tyrosinase; Aromatic Hydroxylation	p. 382
16.3.3 Galactose Oxidase Models	p. 383
16.3.4 CcO Modeling: Heme-Copper Dioxygen Complexes	p. 385
16.3.5 Blue Copper Type 1 (T1) Models	p. 387
16.4 Summary of Key Concepts	p. 388
16.5 Open Questions and Directions for Future Research	p. 389
16.5.1 Copper-Dioxygen Chemistry	p. 389
16.5.2 Models for Active-Site Crosslinked Amino-Acid Residues	p. 390
16.5.3 Cytochrome c Oxidase Models	p. 390
16.5.4 Blue (T1) and Purple (Cu[subscript A]) Models	p. 390
References	p. 391
17 Model Complexes for Zinc-Containing Enzymes	p. 397
17.1 Introduction	p. 398
17.1.1 Coordination Motifs	p. 398
17.1.2 Ligand Geometries	p. 399
17.1.3 Classification of Mononuclear Zinc Peptidases	p. 403
17.2 Mononuclear Zinc Enzymes and Models	p. 405
17.2.1 Zinc Enzymes with a [His[subscript 3]] Motif and Their Model Complexes	p. 405
17.2.1.1 Metzincins	p. 405
17.2.1.2 Carbonic Anhydrase	p. 406
17.2.1.3 Zinc Complexes with Hydridotris(pyrazol-1-yl)borate	p. (Tp) Ligands
17.2.1.4 Zinc Complexes with Neutral N,N,N Ligands	p. 410
17.2.2 Zinc Enzymes with a 2-His-1-Carboxylate Motif and Their Models	p. 410
17.2.2.1 Gluzincins and Aspzincins	p. 412
17.2.2.2 Carboxypeptidases	p. 413
17.2.2.3 Zinc Complexes with N,N,O Ligands	p. 414
17.2.3 Liver Alcohol Dehydrogenase and Models	p. 417
17.2.4 5-Aminolevulinic Acid Dehydratase and Adenosine Deaminase DNA Repair Protein	p. 420
17.3 Dinuclear Zinc Enzymes and Models	p. 422
17.3.1 Metallo[Beta]-Lactamases	p. 423
17.3.2 Aminopeptidases	p. 425
17.3.3 Alkaline Phosphatases and Purple Acid Phosphatase	p. 426
17.4 Conclusions	p. 429
References	p. 429
Subject Index	p. 433

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