Spin States in Biochemistry and Inorganic Chemistry: Influence on Structure and Reactivity

It has long been recognized that metal spin states play a central role in the reactivity of important biomolecules, in industrial catalysis and in spin crossover compounds. As the fields of inorganic chemistry and catalysis move towards the use of cheap, non–toxic first row transition metals, it is essential to understand the important role of spin states in  influencing molecular structure, bonding and reactivity. Spin States in Biochemistry and Inorganic Chemistry provides a complete picture on the importance of spin states for reactivity in biochemistry and inorganic chemistry, presenting both theoretical and experimental perspectives. The successes and pitfalls of theoretical methods such as DFT, ligand–field theory and coupled cluster theory are discussed, and these methods are applied in studies throughout the book. Important spectroscopic techniques to determine spin states in transition metal complexes and proteins are explained, and the use of NMR for the analysis of spin densities is described. Topics covered include:  DFT and ab initio wavefunction approaches to spin states  Experimental techniques for determining spin states  Molecular discovery in spin crossover  Multiple spin state scenarios in organometallic reactivity and gas phase reactions  Transition–metal complexes involving redox non–innocent ligands  Polynuclear iron sulfur clusters  Molecular magnetism  NMR analysis of spin densities This book is a valuable reference for researchers working in bioinorganic and inorganic chemistry, computational chemistry, organometallic chemistry, catalysis, spin–crossover materials, materials science, biophysics and pharmaceutical chemistry. INDICE: About the Editors yyy .Contributors zzz .Foreword by Jeremy Harvey xxx .Acknowledgements .1. General Introduction to Spin States 1M. Swart and M. Costas .1.1 Introduction 2 .1.2 Experimental chemistry: reactivity, synthesis and spectroscopy 3 .1.3 Computational chemistry: quantum–chemistry and basis sets 5 .1.4 References 7 .2. Application of Density Functional and Density Functional Based Ligand Field Theory to Spin States 1C. Daul, M. Zlatar, M. Gruden–Pavloviæ and M. Swart .2.1 Introduction 2 .What is the problem with theory? 5 .2.2 Density Functional Theory 6 .2.2.1 Brief overview of Density Functional Approximations 7 .2.3 Ligand–Field Theory: Bridging the gap between experimental and computational coordination chemistry 9 .2.3.1 Density Functional based Ligand–Field theory 13 .Validation and application studies 18 .2.4 Use of OPBE, SSB–D and S12g density functionals for spin–state splittings 22 .2.4.1 Iron(II) systems: [Fe(H2O)6]2+, [Fe(NH3)6]2+, [Fe(bpy)3]2+, [Fe(amp)2Cl2], [Fe(dpa)2]2+ 23 .2.4.2 Chloro–iron(III) porphyrin 26 .2.4.3 Heptacoordinated complexes 28 .2.4.4 [Co(TACN)2]2+ and [Co(Tp)2] 30 .2.5 Application of LF–DFT 30 .2.5.1 [CrF6]3– 31 .2.5.2 [MnF6]4– 32 .2.5.3 Electronic spectra of iron(II) complexes 33 .2.6 Concluding remarks 39 .2.7 Acknowledgments 40 .2.8 References 41 .3. Ab Initio Wavefunction Approaches to Spin States 1C. Sousa and C. de Graaf .3.1 Introduction and Scope 2 .3.2 Wavefunction based methods for spin states 2 .3.2.1 Single reference methods 3 .3.2.2 Multireference methods 4 .3.2.3 MR perturbation theory 6 .3.2.4 Variational approaches 7 .3.2.5 Density Matrix Renormalization Group theory 8 .3.3 Spin Crossover 8 .3.3.1 Choice of active space and basis set 9 .3.3.2 The HS–LS energy difference 10 .3.3.3 Light–induced excited spin state trapping (LIESST) 13 .3.3.4 Spin crossover in other metals 14 .3.4 Magnetic coupling 16 .3.5 Spin states in biochemical and biomimetic systems 18 .3.6 Two–state reactivity 19 .3.7 Concluding remarks 20 .3.8 References 21 .4. Experimental Techniques for Determining Spin States 1C. Duboc and M. Gennari .4.1 Introduction 2 .4.2 Magnetic measurements 5 .4.3 EPR spectroscopy 9 .4.4 Mössbauer spectroscopy 12 .4.5 X–ray spectroscopic techniques 15 .4.6 NMR spectroscopy 18 .4.7 Other techniques 20 .4.8 Appendix 21 .4.8.1 Theoretical Background 21 .4.8.2 List of Symbols 22 .4.9 References 23 .5. Molecular Discovery in Spin Crossover 1R.J. Deeth .5.1 Introduction 3 .5.2 Theoretical background 3 .5.2.1 Spin transition curves 7 .5.2.2 Light–induced excited spin state trapping 8 .5.3 SCO Systems: Fe(II) 9 .5.4 SCO in non–d6 systems 13 .5.5 Computational methods 15 .5.6 Outlook 20 .5.7 References 22 .6. Multiple Spin State Scenarios in Organometallic Reactivity 1W.I. Dzik, W. Böhmer and B. de Bruin .6.1 Introduction 3 .6.2 Spin–forbidden reactions and two–state reactivity 4 .6.3 Spin state changes in transition metal complexes 8 .6.3.1 Influence of the spin state on the kinetics of ligand exchange 8 .6.3.2 Stoichiometric bond making and breaking reactions 10 .6.3.2.1 Reactivity in the gas phase 10 .6.3.2.2 Reactivity in the condensed phase 13 .6.3.2.2.1 C H bond activation 13 .6.3.2.2.2 –hydride elimination 15 .6.3.3 Spin state situations involving redox–active ligands 17 .6.4 Spin state changes in catalysis 21 .6.4.1 Catalytic (cyclo)oligomerizations 21 .6.4.1.1 Cobalt catalysed cyclotrimerizations 21 .6.4.2 Phillips Cr(II)/SiO2 catalyst 25 .6.4.3 SNS–CrCl3 catalyst 27 .6.5 Concluding remarks 29 .6.6 References 30 .7. Principles and Prospects of Spin–States Reactivity in Chemistry and Bioinorganic Chemistry 1D. Usharani, B. Wang, D.A. Sharon and S. Shaik .7.1 Introduction .7.2 Spin States Reactivity .7.2.1 Two State and Multi State Reactivity .7.2.1.1 The Puzzle that Triggered the Formulation of TSR .7.2.1.2 Spin–State Reactivity Scenarios in Various Bond Activation Reactions .7.2.1.3 Spin–State Reactivity Patterns in Nonheme Type Metal–oxo Complexes .7.2.2 Origins of Spin–Selective Reactivity: Exchange–enhanced Reactivity (EER) and Orbital Selection Rules .7.2.2.1 Consideration of Exchange Interactions .7.2.2.2 The Impact of Variable Exchange Interactions During H–abstraction .7.2.3 Considerations of EER vs. OCR .7.2.3.1 Usage of Electron–Shift Diagrams to Predict the Preferred Pathway and Transition State Structures for H–Abstraction .7.2.3.2 The Predicted Pathway Is Typified by EER and an Upright 5TSH Species .7.2.4 Consideration of Spin–State Selectivity in H–Abstraction: The Power of EER .7.2.4.1 The Strength of the EER Rule .7.2.4.2 Frontier Orbital Interactions as Alternative Rationales for Spin–State Selectivity .7.2.4.3 Dependence of EER and Spin–State Selectivity on the Transition Metal and the d–Electron Count .7.2.5 The Origins of Mechanistic Selection – Why Are C–H Hydroxylations Stepwise Processes? .7.3 Prospects of TSR and MSR .7.3.1 Probing Spin State Reactivity .7.3.1.1 Direct Evaluation of Spin State Reactivity .7.3.1.2 Usage of Kinetic Isotope Effect (KIE) as a Probe of Spin State Reactivity .7.3.2 Are Spin Inversion Probabilities Useful for Analyzing TSR? .7.4 Concluding Remarks .7.5 References .8. Multiple Spin State Scenarios in Gas Phase Reactions 1J. Roithová .8.1 Introduction .8.2 Experimental methods for the investigation of metal–ion reactions .8.3 Multiple state reactivity: Reactions of metal cations with methane .8.4 Effect of the oxidation state: Reactions of metal hydride cations with methane .8.5 Two–state reactivity: Reactions of metal oxide cations .8.6 Effect of ligands .8.7 Effect of non–innocent ligands .8.8 Concluding Remarks .8.9 References .9. Catalytic function and mechanism of heme and nonheme iron(IV)–oxo complexes in nature1M.G. Quesne, A.S. Faponle, D.P. Goldberg and S.P. de Visser .9.1 Introduction 3 .9.2 Cytochrome P450 enzymes 4 .9.2.1 Importance of Cytochrome P450 Enzymes 5 .9.2.2 P450 Activation of Long–Chain Fatty Acids 6 .9.2.3 Heme Monooxygenases and Peroxygenases 6 .9.2.4 Catalytic Cycle of Cytochrome P450 Enzymes 7 .9.3 Nonheme Iron Dioxygenases 8 .9.3.1 Cysteine dioxygenase. 10 .9.3.2 AlkB repair enzymes. 11 .9.3.3 Nonheme iron halogenases. 14 .9.4 Conclusions 17 .9.5 Acknowledgements 17 .9.6 References 18 .10. Terminal Metal Oxo Species with Unusual Spin States 1S.A. Cook, D.C. Lacy and A.S. Borovik .10.1 Introduction .10.2 Bonding .10.2.1 Bonding Considerations: Tetragonal Symmetry .10.2.2 Bonding Considerations: Trigonal Symmetry .10.2.3 Methods of Characterization .10.3 Case studies .10.3.1 Iron oxo Chemistry .10.3.1.1 Biological Examples .10.3.1.2 FeIII Oxo Complexes .10.3.1.3 FeIV Oxo Complexes .10.3.1.4 EPR Spectroscopy on FeIV Oxo Complexes .10.3.1.5 FeV Oxo Complexes .10.3.2 Manganese oxo Chemistry .10.3.2.1 Biological Examples .10.3.2.2 MnIII Oxo Complexes .10.3.2.3 MnIV Oxo Complexes .10.3.2.4 MnV Oxo Complexes .10.3.2.5 EPR Spectroscopy of Mn oxo Complexes .10.3.3 Cautionary Tales: Late Transition Metal Oxido Complexes .10.3.4 Effects of Redox Inactive Metal Ions .10.3.5 Metal Oxyl Complexes .10.4 Reactivity .10.4.1 General Concepts: Proton versus Electron Transfer .10.4.2 Spin State and Reactivity .10.5 Summary .10.6 References .11. Multiple Spin Scenarios in Transition–Metal Complexes Involving Redox Non–Innocent Ligands 1F. Heims and K. Ray .11.1 Introduction 3 .11.2 Survey of Non–Innocent Ligands 5 .11.3 Identification of Non–Innocent Ligands 8 .11.3.1 X–ray Crystallography 8 .11.3.2 EPR spectroscopy 9 .11.3.3 Mössbauer spectroscopy 11 .11.3.4 XAS spectroscopy 11 .11.4 Selected Examples of Biological and Chemical Systems Involving Non–innocent Ligands 13 .11.4.1 Copper–radical interaction: 13 .11.4.1.1 Biological Catalysis: 13 .11.4.1.2 Chemical Catalysis 21 .11.4.2 Iron–radical interaction: 25 .11.5 Concluding Remarks 32 .12. Molecular Magnetism 1G. Aromí, P. Gamez and O. Roubeau .12.1 Introduction .12.2 Molecular magnetism: motivations, early achievements and foundations .12.3 Molecular Nanomagnets (MNM) .12.3.1 Single Molecule Magnets (SMM) .12.3.2 Single Chain Magnets (SCM) .12.3.3 Single Ion Magnets (SIM) .12.4 Switchable systems .12.4.1 Spin Crossover (SCO) .12.4.2 Valence Tautomerism (VT) .12.4.3 Charge Transfer (CT) .12.4.4 Light–Driven Ligand–induced Spin Change (LD–LISC) .12.4.5 Photoswitching (PS) through intermetallic Charge Transfer .12.5 Molecular–based magnetic refrigerants .12.5.1 The magneto–caloric effect, its experimental determination and key parameters .12.5.2 Molecular to extended framework coolers towards applications .12.6 Quantum Manipulation of the Electronic Spin for Quantum Computing .12.6.1 Organic Radicals .12.6.2 Transition Metal Clusters .12.6.3 Lanthanides as realization of Qubits .12.6.4 Engineering of Molecular Quantum Gates with Lanthanide Qubits .12.7 Perspectives towards applications and concluding remarks .13. Electronic Structure, Bonding, Spin Coupling, and Energetics of Polynuclear Iron Sulfur Clusters A Broken Symmetry Density Functional Theory Perspective 1K.H. Hopmann, V. Pelmenschikov, W.–G. Han Du and L. Noodleman .13.1 Introduction .13.2 Fe–S Coordination Geometric and Electronic Structure .13.3 Spin Polarization Splitting and the Inverted Level Scheme .13.4 Spin Coupling and the Broken Symmetry Method .13.5 Electron Localization and Delocalization .13.6 Polynuclear Systems–Competing Heisenberg Interactions and Spin–Dependent Delocalization .13.7 Preamble to Three Major Topics: Iron–sulfur–nitrosyls, Adenosine–5–phosphosulfate Reductase, and the Proximal Cluster of Membrane–Bound NiFe–Hydrogenase .13.7.1 Nonheme Iron Nitrosyl Complexes .13.7.2 Adenosine–5–phosphosulfate Reductase (APSR) .13.7.3 Proximal Cluster of O2–Tolerant Membrane–Bound [NiFe]–Hydrogenase in Three Redox States. .13.8 Concluding Remarks .14. Environment Effects on Spin States, Properties and Dynamics from Multi–Level QM/MM Studies1A. Petrenko and M. Stein .14.1 Introduction 2 .14.1.1 Environmental Effects 4 .14.1.2 Hybrid QM/MM Embedding Schemes 5 .14.2 The Quantum Spin Hamiltonian– Linking Theory and Experiment 11 .14.3 The Solvent as an Environment 15 .14.3.1 FTIR 16 .14.3.2 NMR 16 .14.3.3 EPR 17 .14.4 Effect of different levels of QM and MM treatment 20 .14.4.1 Convergence and caveats at the QM level 20 .14.4.2 Accuracy of the MM part 23 .14.4.3 QM vs. QM/MM Methods 24 .14.5 Illustrative Bioinorganic Examples 26 .14.5.1 Cytochrome P450 27 .14.5.1.1 The effect of the protein environment on the heme spin state – Spin conversion from resting and substrate–bound states 29 .14.5.1.2 Compound I 31 .14.5.2 Hydrogenase Enzymes 37 .14.5.2.1 [NiFe] Hydrogenases 38 .14.5.2.2 [FeFe] Hydrogenases 42 .14.5.3 Photosystem II and the effect of QM size 44 .14.6 From static spin–state properties to dynamics and kinetic of electron transfer 49 .14.7 Final Remarks and Conclusions 53 .14.8 Acknowledgements 58 .14.9 References 58 .15. High–spin and low–spin states in {FeNO}7, FeIV=O, and FeIII–OOH complexes and their correlations to reactivity 1E.I. Solomon, K.D. Sutherlin and M. Srnec .15.1 Introduction .15.2 High–spin and low–spin {FeNO}7 complexes: correlations to O2 activation .15.2.1: Spectroscopic definition of the electronic structure of HS {FeNO}7 .15.2.2 Computational studies of S = 3/2 {FeNO}7 complexes and related {FeO2}8 complexes .15.2.3 Extension to IPNS and HPPD: implications for reactivity .15.2.4 Correlation to {FeNO}7 S = 1/2 .15.3 Low–spin (S = 1) and high–spin (S = 2) FeIV=O complexes .15.3.1 FeIV=O S = 1 complexes: ? FMO .15.3.2 FeIV=O S = 2 sites: ? and ? FMOs .15.3.3 Contributions of FMOs to reactivity .15.4 Low–spin (S = 1/2) and high–spin (S = 5/2) FeIII OOH complexes .15.4.1 Spin state dependence of O O bond homolysis .15.4.2 FeIII OOH S = 1/2 reactivity: ABLM .15.4.3 FeIII OOH spin state dependent reactivity: FMOs .15.5 Conclusion .16. NMR Analysis of Spin Densities 1K. Bren .16.1 Introduction and Scope .16.2 Spin Density Distribution in Transition Metal Complexes .16.3 NMR of Paramagnetic Molecules .16.3.1 Chemical Shifts .16.3.2 Relaxation Rates .16.4 Analysis of Spin Densities by NMR .16.4.1 Factoring Contributions to Hyperfine Shifts .16.4.2 Relaxation Properties and Spin Density .16.4.3 DFT Approaches to Analyzing Hyperfine Shifts .16.4.4 Natural Bond Orbital Analysis .16.4.5 Application and Practicalities .16.5. Probing Spin Density in Paramagnetic Metalloproteins .16.5.1 Heme Proteins .16.5.2 Iron–sulfur Clusters .16.5.3 Copper Proteins .16.6 Conclusions and Outlook .16.7 References .17. Summary and Outlook 1M. Costas and M. Swart .17.1 Summary 2 .17.2 Outlook 2 .17.3 References 3 .Index

• ISBN: 978-1-118-89831-4
• Editorial: Wiley–Blackwell
• Encuadernacion: Cartoné
• Páginas: 472
• Fecha Publicación: 11/12/2015
• Nº Volúmenes: 1
• Idioma: Inglés