Additional Information
Book Details
Abstract
There has been enormous progress in our understanding of molybdenum and tungsten enzymes and relevant inorganic complexes of molybdenum and tungsten over the past twenty years. This set of three books provides a timely and comprehensive overview of the field and documents the latest research.
Building on the first and second volumes that focussed on biochemistry and bioinorganic chemistry aspects, the third volume focusses on spectroscopic and computational methods that have been applied to both enzymes and model compounds. A particular emphasis is placed on how these important studies have been used to reveal critical components of enzyme mechanisms.
This text will be a valuable reference to workers both inside and outside the field, including graduate students and young investigators interested in developing new research programs in this area.
This book is edited by Professor Russ Hille (University of California, Riverside), Professor Carola Schulzke (University of Greifswald) and Professor Martin Kirk (University of New Mexico) who have over 275 publications ad over 65 years of experience between them in the field. Their complementary expertise in molybdenum containing enzymes, bioinorganic chemistry and the physical inorganic chemistry of molybdenum complexes and enzymes, respectively, allow the authoritative and comprehensive coverage demonstrated in this book.
Table of Contents
| Section Title | Page | Action | Price |
|---|---|---|---|
| Cover | Cover | ||
| Molybdenum and Tungsten Enzymes Spectroscopic and Theoretical Investigations | i | ||
| Preface | v | ||
| Dedication | vii | ||
| Contents | ix | ||
| Chapter 1 - Spectroscopic and Electronic Structure Studies Probing Mechanism: Introduction and Overview | 1 | ||
| 1.1 Introduction | 1 | ||
| 1.2 Overview | 2 | ||
| 1.2.1 Pyranopterin Molybdenum Enzymes | 2 | ||
| 1.2.2 Nitrogenase | 8 | ||
| 1.3 Summary | 9 | ||
| Acknowledgements | 10 | ||
| References | 10 | ||
| Chapter 2 - Spectroscopic and Electronic Structure Studies of Mo Model Compounds and Enzymes | 13 | ||
| 2.1 Introduction and Scope | 13 | ||
| 2.2 The Pyranopterin Dithiolene and the Molybdenum Cofactor (Moco) | 16 | ||
| 2.2.1 General Background | 16 | ||
| 2.2.2 Model Studies Defining the Mo–Dithiolene Interaction in Moco | 17 | ||
| 2.2.3 Conformational Studies of the PDT | 23 | ||
| 2.2.4 Spectroscopic Studies of the PDT | 24 | ||
| 2.3 Sulfite Oxidase | 26 | ||
| 2.3.1 Active Site Structure and General Reaction Catalyzed | 26 | ||
| 2.3.2 Select Spectroscopic Studies of Model Systems | 28 | ||
| 2.3.3 Spectroscopic Studies of SO and SO-Type Enzymes | 31 | ||
| 2.3.4 Active Site Electronic Structure Contributions to Reactivity | 33 | ||
| 2.4 Xanthine Oxidoreductase (XOR) | 35 | ||
| 2.4.1 Active Site Structure and General Reaction Catalyzed | 35 | ||
| 2.4.2 Select Spectroscopic Studies of Model Systems | 36 | ||
| 2.4.3 Spectroscopic Studies of XOR | 38 | ||
| 2.4.4 Active Site Electronic Structure Contributions to Reactivity | 39 | ||
| 2.5 Carbon Monoxide Dehydrogenase | 41 | ||
| 2.5.1 Active Site Structure and General Reaction Catalyzed | 41 | ||
| 2.5.2 EPR Spectroscopic Studies of a Key Model System | 42 | ||
| 2.5.3 Spectroscopic Studies of CODH | 43 | ||
| 2.5.4 Active Site Electronic Structure Contributions to Reactivity | 45 | ||
| 2.6 Dimethylsulfoxide (DMSO) Reductase | 47 | ||
| 2.6.1 Active Site Structure and General Reaction Catalyzed | 47 | ||
| 2.6.2 Select Spectroscopic Studies of Model Systems | 48 | ||
| 2.6.3 Spectroscopic Studies of DMSOR | 50 | ||
| 2.6.4 Active Site Electronic Structure Contributions to Reactivity | 52 | ||
| 2.7 MOSC Family Enzymes | 53 | ||
| 2.7.1 Active Site Structure and General Reaction Catalyzed | 53 | ||
| 2.7.2 Spectroscopic Studies of MOSC Proteins | 55 | ||
| 2.7.3 Active Site Electronic Structure Contributions to Reactivity | 56 | ||
| 2.8 Perspective | 58 | ||
| Acknowledgements | 59 | ||
| References | 59 | ||
| Chapter 3 - Electron Paramagnetic Resonance Studies of Molybdenum Enzymes | 68 | ||
| 3.1 Introduction | 68 | ||
| 3.2 Principles of EPR Techniques and Application to Mo/W Enzymes | 69 | ||
| 3.2.1 Basis of EPR Spectroscopy | 69 | ||
| 3.2.2 EPR Properties of Mo and W Enzymes | 72 | ||
| 3.3 g-Tensor Analysis for Mo/W Enzymes | 75 | ||
| 3.3.1 g-Tensor for a d1 Configuration | 75 | ||
| 3.3.2 Magneto-Structural Correlations in the Mo-Enzyme Family | 76 | ||
| 3.3.3 g-Tensor Analysis of Mo-bisPGD Active Site: Influence of the Protein Ligands | 78 | ||
| 3.3.4 The g-Tensor of Mo(V)-monoPPT: The Case Study of the Sulfite Oxidase Family | 81 | ||
| 3.3.5 g-Tensor and Substrate Binding: The Xanthine Oxidase Family | 82 | ||
| 3.3.6 g-Tensor Calculation: Ab-initio and DFT Methods | 83 | ||
| 3.3.7 g-Tensor of W(v) Species in Tungsten Enzymes | 85 | ||
| 3.4 Detection and Analysis of Hyperfine Couplings to Mo/W(v) Species | 86 | ||
| 3.4.1 Hyperfine Coupling to the Metal Ion | 86 | ||
| 3.4.1.1 95,97Mo Hyperfine and Nuclear Quadrupole Tensors | 86 | ||
| 3.4.1.2 183W Hyperfine Couplings | 88 | ||
| 3.4.2 Superhyperfine Couplings to the Mo(v) Species in Xanthine Oxidase Enzyme Family | 90 | ||
| 3.4.2.1 33S Hyperfine Couplings to Mo(v): Detection of Directly Coordinated Sulfur Ligands | 90 | ||
| 3.4.2.2 13C Hyperfine Couplings: Detection of Substrate/Inhibitors in the Vicinity of the Mo(v) Ion | 90 | ||
| 3.4.2.3 Detection of 14N Interactions with Substrates and Inhibitors | 94 | ||
| 3.4.2.4 Isotopic Substitution Studies with 17O | 94 | ||
| 3.4.2.5 75As and 199,201Hg Hyperfine Couplings to Arsenite- and p-CMB-Inhibited Mo(v) Forms | 95 | ||
| 3.4.2.6 31P Hyperfine Couplings | 96 | ||
| 3.4.3 Superhyperfine Couplings to Mo(v) Species Formed in Sulfite Oxidase Enzyme Family | 96 | ||
| 3.4.3.1 Elucidating the Structure of the High-pH and Low-pH Mo(v) Species Using 1H, 17O and 35,37Cl Hyperfine Couplings | 96 | ||
| 3.4.3.1.1\rDetection and Analysis of 1H and 17O Hyperfine Interactions.The molybdenum cofactor of chicken liver sulfite oxidase (cSO) was r... | 96 | ||
| 3.4.3.1.2\r35,37Cl hfi to the Low-pH Mo(v) Species.The pKa for interconversion between the hpH and the lpH forms is raised by the presence ... | 100 | ||
| 3.4.3.1.3\rEPR and ENDOR Studies on Sulfane Dehydrogenase.Mo(v) species generated in sulfane dehydrogenase (SoxCD1) from Paracoccus pantotr... | 101 | ||
| 3.4.3.2 31P and 75As Hyperfine Interactions to the Phosphate- and Arsenate-Inhibited Mo(v) Species | 101 | ||
| 3.4.3.3 33S Hyperfine Interactions | 102 | ||
| 3.4.3.3.1\rThe Blocked (Sulfite) Mo(v) Species.Measurements of 33S hyperfine couplings to Mo(v) have been extensively carried out on the bl... | 102 | ||
| 3.4.3.3.2\r33S-labelled Molybdenum Cofactor.The possibility of direct incorporation of 33S into PPT using controlled in vitro synthesis wit... | 103 | ||
| 3.4.4 Superhyperfine Couplings to the Mo(v) Species in Mo/W-bisPGD Enzymes | 104 | ||
| 3.4.4.1 High-pH and Low-pH Mo(v) Species in Respiratory Nitrate Reductases | 104 | ||
| 3.4.4.2 Non-exchangeable 1H Couplings to the High-g Mo(v) Species in Periplasmic Nitrate Reductases | 105 | ||
| 3.4.4.3 Superhyperfine Couplings to the Mo(v) Species in Formate Dehydrogenases | 106 | ||
| 3.4.4.4 The Structure of the Mo(v) Species in mARC | 107 | ||
| 3.5 Detection and Analysis of Spin–Spin Interactions between the Mo Cofactor and other Metal Centres | 108 | ||
| 3.6 Concluding Remarks | 110 | ||
| Acknowledgements | 112 | ||
| References | 112 | ||
| Chapter 4 - X-Ray Absorption Spectroscopy of Molybdenum and Tungsten Enzymes | 121 | ||
| 4.1 Introduction | 121 | ||
| 4.2 The Physical Basis of X-Ray Absorption Spectroscopy | 122 | ||
| 4.2.1 The EXAFS | 125 | ||
| 4.2.2 The Fourier Transform | 128 | ||
| 4.2.3 Determination of Structural Parameters from the EXAFS | 129 | ||
| 4.2.4 Confusion of EXAFS Backscatterers | 134 | ||
| 4.2.5 EXAFS Cancellation | 134 | ||
| 4.2.6 Multiple Scattering | 134 | ||
| 4.2.7 The EXAFS Resolution and the Debye–Waller Term | 134 | ||
| 4.2.8 Number of Independent Variables | 136 | ||
| 4.3 Experimental Aspects of XAS | 137 | ||
| 4.3.1 Sample Preparation | 140 | ||
| 4.3.2 Data Acquisition Strategies | 142 | ||
| 4.3.3 Fluorescence Self-Absorption Effects | 143 | ||
| 4.3.4 Combining XAS with Other Methods – A Holistic Approach | 144 | ||
| 4.4 The DMSO Reductase Family of Mo and W Enzymes | 145 | ||
| 4.4.1 DMSO Reductase | 145 | ||
| 4.4.2 Arsenite Oxidase | 149 | ||
| 4.4.3 The Archaeal Tungsten Enzymes | 150 | ||
| 4.4.4 Other DMSO Reductase Family Members | 151 | ||
| 4.5 The Xanthine Oxidase Family of Mo Enzymes | 152 | ||
| 4.5.1 Xanthine Oxidase | 152 | ||
| 4.5.2 Carbon Monoxide Dehydrogenase | 153 | ||
| 4.6 The Sulfite Oxidase Family of Mo Enzymes | 154 | ||
| 4.7 Nitrogenase | 158 | ||
| 4.8 Concluding Remarks | 161 | ||
| Acknowledgements | 161 | ||
| References | 162 | ||
| Chapter 5 - Electrochemistry of Molybdenum and Tungsten Enzymes | 168 | ||
| 5.1 Introduction | 168 | ||
| 5.1.1 The Mo and W Enzyme Families | 168 | ||
| 5.1.2 Enzyme Electrochemistry | 169 | ||
| 5.2 Xanthine Oxidase Family | 172 | ||
| 5.2.1 Xanthine Oxidoreductase | 172 | ||
| 5.2.2 Aldehyde Oxidoreductase | 180 | ||
| 5.3 Sulfite Oxidase Family | 181 | ||
| 5.3.1 Sulfite Oxidoreductase | 182 | ||
| 5.3.1.1 Bacterial Sulfite Dehydrogenase | 183 | ||
| 5.3.1.2 Chicken Sulfite Oxidase | 188 | ||
| 5.3.1.3 Human Sulfite Oxidase | 190 | ||
| 5.3.2 Eukaryotic Nitrate Reductase | 192 | ||
| 5.3.2.1 Plant Nitrate Reductase | 193 | ||
| 5.3.2.2 Fungal Nitrate Reductase | 195 | ||
| 5.3.2.3 Algal Nitrate Reductase | 196 | ||
| 5.4 DMSO Reductase Family | 196 | ||
| 5.4.1 DMSO Reductase | 197 | ||
| 5.4.2 DMS Dehydrogenase | 203 | ||
| 5.4.3 Bacterial Nitrate Reductase | 203 | ||
| 5.4.3.1 Periplasmic Nitrate Reductase (NapAB) | 204 | ||
| 5.4.3.2 Respiratory Nitrate Reductase (NarGHI) | 206 | ||
| 5.4.4 Arsenite Oxidase | 208 | ||
| 5.4.5 Ethylbenzene Dehydrogenase | 211 | ||
| 5.4.6 Formate Dehydrogenase | 212 | ||
| 5.4.7 Glyceraldehyde 3-Phosphate Oxidoreductase | 214 | ||
| 5.5 Conclusions | 214 | ||
| Acknowledgement | 215 | ||
| References | 215 | ||
| Chapter 6 - Nitrogen Fixation in Nitrogenase and Related Small-Molecule Models: Results of DFT Calculations | 223 | ||
| 6.1 Introduction | 223 | ||
| 6.1.1 Structure and Function of Nitrogenase | 224 | ||
| 6.1.2 Fe-Protein Cycle | 224 | ||
| 6.1.3 Metal Clusters Within the MoFe-Protein | 226 | ||
| 6.1.4 Thorneley–Lowe Cycle | 227 | ||
| 6.1.5 Site-Directed Mutagenesis Experiments | 227 | ||
| 6.1.6 Trapping and Spectroscopic Characterization of Intermediates of N2 Reduction: Towards an Experimentally Derived Mechanism o... | 228 | ||
| 6.2 DFT Treatments of N2 Reduction in Model Systems | 229 | ||
| 6.2.1 Schrock Cycle | 231 | ||
| 6.2.2 Nishibayashi’s System | 238 | ||
| 6.2.3 Chatt Cycle | 239 | ||
| 6.2.4 Reduction and Protonation of N2 at Cubane Clusters | 241 | ||
| 6.2.5 Reduction and Protonation of N2 at Iron Complexes | 242 | ||
| 6.3 DFT Calculations on the FeMoco and its Reactivity with N2 | 246 | ||
| 6.3.1 Noodleman and Coworkers | 246 | ||
| 6.3.2 Nørskov and Coworkers | 252 | ||
| 6.3.3 Blöchl, Kästner et al | 256 | ||
| 6.3.4 Dance | 259 | ||
| 6.3.5 Further Theoretical Studies | 261 | ||
| 6.3.6 Mo(iii) Charge State of FeMoco | 264 | ||
| 6.4 Summary and Conclusions | 266 | ||
| Acknowledgement | 266 | ||
| References | 267 | ||
| Chapter 7 - Computational Studies of Molybdenum and Tungsten Enzymes | 275 | ||
| 7.1 Introduction | 275 | ||
| 7.2 Computational Methods to Study Metalloenzymes | 279 | ||
| 7.2.1 QM Methods | 280 | ||
| 7.2.2 Hybrid QM/QM Calculations | 283 | ||
| 7.2.3 QM-Cluster Calculations | 283 | ||
| 7.2.4 QM/MM Calculations | 284 | ||
| 7.2.5 How to Model the MPT Ligand | 287 | ||
| 7.3 DMSO Reductase | 289 | ||
| 7.4 Sulfite Oxidase | 298 | ||
| 7.5 Xanthine Oxidase | 306 | ||
| 7.6 Comparison of the Three Families | 311 | ||
| 7.7 Conclusions | 314 | ||
| Acknowledgements | 316 | ||
| References | 316 | ||
| Subject Index | 322 |