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Computational modeling for homogeneous and enzymatic catalysis [[electronic resource] ] : a knowledge-base for designing efficient catalysts / / edited by Keiji Morokuma and Djamaladdin G. Musaev
| Computational modeling for homogeneous and enzymatic catalysis [[electronic resource] ] : a knowledge-base for designing efficient catalysts / / edited by Keiji Morokuma and Djamaladdin G. Musaev |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
| Descrizione fisica | 1 online resource (400 p.) |
| Disciplina | 660.2995 |
| Altri autori (Persone) |
MorokumaK <1934-> (Keiji)
MusaevDjamaladdin G |
| Soggetto topico |
Catalysis - Computer simulation
Catalysts |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-282-37223-8
9786612372230 3-527-62196-2 3-527-62197-0 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Computational Modeling for Homogeneous and Enzymatic Catalysis; Contents; Preface; List of Contributors; 1 Computational Insights into the Structural Properties and Catalytic Functions of Selenoprotein Glutathione Peroxidase (GPx); 1.1 Introduction; 1.2 Catalytic Functions; 1.2.1 Peroxidase Activity; 1.2.2 Reductase Activity; 1.3 Computational Details; 1.3.1 Computational Methods; 1.3.2 Computational Models; 1.4 Results and Discussion; 1.4.1 Refinement of the Active Site; 1.4.2 Catalytic Functions: Peroxidase Activity
1.4.3 Catalytic Functions: Effect of the Surrounding Protein on the Peroxidase Activity1.4.3.1 Hydrogen Peroxide Coordination; 1.4.3.2 Formation of Selenenic Acid [E-Se-OH]; 1.4.4 Catalytic Functions: Reductase Activity; 1.4.4.1 Peroxynitrite/Peroxynitrous Acid (ONOO ̄/ONOOH) Coordination; 1.4.4.2 Oxidation Pathway; 1.4.4.3 Nitration Pathways; 1.5 Summary; References; 2 A Comparison of Tetrapyrrole Cofactors in Nature and their Tuning by Axial Ligands; 2.1 Introduction; 2.2 Methodology; 2.3 Comparison of the Intrinsic Chemical Properties of the Tetrapyrroles; 2.3.1 Introduction 2.3.2 Spin States2.3.3 Tetrapyrroles Prefer Their Native Ions; 2.3.4 Cavity Size and Flexibility of the Tetrapyrroles; 2.3.5 Cytochrome-like Electron Transfer; 2.3.6 Stability of a Metal-Carbon Bond; 2.3.7 Metallation Reaction; 2.4 Tuning of Tetrapyrrole Structure and Function by Axial Ligands; 2.4.1 Introduction; 2.4.2 Importance of the Lower Axial Ligand for B(12) Chemistry; 2.4.3 Lower Axial Ligand in Cofactor F430; 2.4.4 Importance of Axial Ligands for the Globins; 2.4.5 Role of Axial Ligands for the Cytochromes; 2.4.6 Role of the Axial Ligand in Heme Enzymes 2.4.7 Tuning the His Ligand by Hydrogen Bonds in Heme Proteins2.4.8 Axial Ligand in Chlorophylls; 2.5 Concluding Remarks; References; 3 Modeling of Mechanisms for Metalloenzymes where Protons and Electrons Enter or Leave; 3.1 Introduction; 3.2 Energy Diagrams; 3.2.1 Photosystem II; 3.2.2 Cytochrome c Oxidase; 3.2.3 Nitric Oxide Reduction; 3.2.4 NiFe-hydrogenase; 3.2.5 Molybdenum CO Dehydrogenase; 3.3 Conclusions; References; 4 Principles of Dinitrogen Hydrogenation: Computational Insights; 4.1 Introduction 4.2 Reaction Mechanism of the Coordinated Dinitrogen Molecule in Di-zirconocene-N(2) Complexes with a Hydrogen Molecule4.2.1 Mechanism of the Reaction (3); 4.2.2 Mechanisms of the Reactions (4) and (5); 4.3 Factors Controlling the N(2) Coordination Modes in the Di-zirconocene-N(2) Complexes; 4.4 Why the [(η(5)-C(5)Me(n)H(5-n))(2)Ti](2)(μ(2),η(2),η(2)-N(2)) Complex Cannot Add a H(2) Molecule to the Side-on Coordinated N(2), while its Zr- and Hf-analogs Can 4.4.1 Relative Stability of the Lowest Singlet (S) and Triplet (T) Electronic States of the Complexes [(η(5)-C(5)Me(n)H(5-n))(2)M](2)(μ(2),η(2),η(2)-N(2)), II_M (for M = Ti, Zr, and Hf, and n = 0 and 4) |
| Record Nr. | UNINA-9910146268003321 |
| Weinheim, : Wiley-VCH | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Computational modeling for homogeneous and enzymatic catalysis [[electronic resource] ] : a knowledge-base for designing efficient catalysts / / edited by Keiji Morokuma and Djamaladdin G. Musaev
| Computational modeling for homogeneous and enzymatic catalysis [[electronic resource] ] : a knowledge-base for designing efficient catalysts / / edited by Keiji Morokuma and Djamaladdin G. Musaev |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
| Descrizione fisica | 1 online resource (400 p.) |
| Disciplina | 660.2995 |
| Altri autori (Persone) |
MorokumaK <1934-> (Keiji)
MusaevDjamaladdin G |
| Soggetto topico |
Catalysis - Computer simulation
Catalysts |
| ISBN |
1-282-37223-8
9786612372230 3-527-62196-2 3-527-62197-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Computational Modeling for Homogeneous and Enzymatic Catalysis; Contents; Preface; List of Contributors; 1 Computational Insights into the Structural Properties and Catalytic Functions of Selenoprotein Glutathione Peroxidase (GPx); 1.1 Introduction; 1.2 Catalytic Functions; 1.2.1 Peroxidase Activity; 1.2.2 Reductase Activity; 1.3 Computational Details; 1.3.1 Computational Methods; 1.3.2 Computational Models; 1.4 Results and Discussion; 1.4.1 Refinement of the Active Site; 1.4.2 Catalytic Functions: Peroxidase Activity
1.4.3 Catalytic Functions: Effect of the Surrounding Protein on the Peroxidase Activity1.4.3.1 Hydrogen Peroxide Coordination; 1.4.3.2 Formation of Selenenic Acid [E-Se-OH]; 1.4.4 Catalytic Functions: Reductase Activity; 1.4.4.1 Peroxynitrite/Peroxynitrous Acid (ONOO ̄/ONOOH) Coordination; 1.4.4.2 Oxidation Pathway; 1.4.4.3 Nitration Pathways; 1.5 Summary; References; 2 A Comparison of Tetrapyrrole Cofactors in Nature and their Tuning by Axial Ligands; 2.1 Introduction; 2.2 Methodology; 2.3 Comparison of the Intrinsic Chemical Properties of the Tetrapyrroles; 2.3.1 Introduction 2.3.2 Spin States2.3.3 Tetrapyrroles Prefer Their Native Ions; 2.3.4 Cavity Size and Flexibility of the Tetrapyrroles; 2.3.5 Cytochrome-like Electron Transfer; 2.3.6 Stability of a Metal-Carbon Bond; 2.3.7 Metallation Reaction; 2.4 Tuning of Tetrapyrrole Structure and Function by Axial Ligands; 2.4.1 Introduction; 2.4.2 Importance of the Lower Axial Ligand for B(12) Chemistry; 2.4.3 Lower Axial Ligand in Cofactor F430; 2.4.4 Importance of Axial Ligands for the Globins; 2.4.5 Role of Axial Ligands for the Cytochromes; 2.4.6 Role of the Axial Ligand in Heme Enzymes 2.4.7 Tuning the His Ligand by Hydrogen Bonds in Heme Proteins2.4.8 Axial Ligand in Chlorophylls; 2.5 Concluding Remarks; References; 3 Modeling of Mechanisms for Metalloenzymes where Protons and Electrons Enter or Leave; 3.1 Introduction; 3.2 Energy Diagrams; 3.2.1 Photosystem II; 3.2.2 Cytochrome c Oxidase; 3.2.3 Nitric Oxide Reduction; 3.2.4 NiFe-hydrogenase; 3.2.5 Molybdenum CO Dehydrogenase; 3.3 Conclusions; References; 4 Principles of Dinitrogen Hydrogenation: Computational Insights; 4.1 Introduction 4.2 Reaction Mechanism of the Coordinated Dinitrogen Molecule in Di-zirconocene-N(2) Complexes with a Hydrogen Molecule4.2.1 Mechanism of the Reaction (3); 4.2.2 Mechanisms of the Reactions (4) and (5); 4.3 Factors Controlling the N(2) Coordination Modes in the Di-zirconocene-N(2) Complexes; 4.4 Why the [(η(5)-C(5)Me(n)H(5-n))(2)Ti](2)(μ(2),η(2),η(2)-N(2)) Complex Cannot Add a H(2) Molecule to the Side-on Coordinated N(2), while its Zr- and Hf-analogs Can 4.4.1 Relative Stability of the Lowest Singlet (S) and Triplet (T) Electronic States of the Complexes [(η(5)-C(5)Me(n)H(5-n))(2)M](2)(μ(2),η(2),η(2)-N(2)), II_M (for M = Ti, Zr, and Hf, and n = 0 and 4) |
| Record Nr. | UNINA-9910830195903321 |
| Weinheim, : Wiley-VCH | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Computational modeling for homogeneous and enzymatic catalysis : a knowledge-base for designing efficient catalysts / / edited by Keiji Morokuma and Djamaladdin G. Musaev
| Computational modeling for homogeneous and enzymatic catalysis : a knowledge-base for designing efficient catalysts / / edited by Keiji Morokuma and Djamaladdin G. Musaev |
| Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
| Descrizione fisica | 1 online resource (400 p.) |
| Disciplina | 660.2995 |
| Altri autori (Persone) |
MorokumaK <1934-> (Keiji)
MusaevDjamaladdin G |
| Soggetto topico |
Catalysis - Computer simulation
Catalysts |
| ISBN |
1-282-37223-8
9786612372230 3-527-62196-2 3-527-62197-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Computational Modeling for Homogeneous and Enzymatic Catalysis; Contents; Preface; List of Contributors; 1 Computational Insights into the Structural Properties and Catalytic Functions of Selenoprotein Glutathione Peroxidase (GPx); 1.1 Introduction; 1.2 Catalytic Functions; 1.2.1 Peroxidase Activity; 1.2.2 Reductase Activity; 1.3 Computational Details; 1.3.1 Computational Methods; 1.3.2 Computational Models; 1.4 Results and Discussion; 1.4.1 Refinement of the Active Site; 1.4.2 Catalytic Functions: Peroxidase Activity
1.4.3 Catalytic Functions: Effect of the Surrounding Protein on the Peroxidase Activity1.4.3.1 Hydrogen Peroxide Coordination; 1.4.3.2 Formation of Selenenic Acid [E-Se-OH]; 1.4.4 Catalytic Functions: Reductase Activity; 1.4.4.1 Peroxynitrite/Peroxynitrous Acid (ONOO ̄/ONOOH) Coordination; 1.4.4.2 Oxidation Pathway; 1.4.4.3 Nitration Pathways; 1.5 Summary; References; 2 A Comparison of Tetrapyrrole Cofactors in Nature and their Tuning by Axial Ligands; 2.1 Introduction; 2.2 Methodology; 2.3 Comparison of the Intrinsic Chemical Properties of the Tetrapyrroles; 2.3.1 Introduction 2.3.2 Spin States2.3.3 Tetrapyrroles Prefer Their Native Ions; 2.3.4 Cavity Size and Flexibility of the Tetrapyrroles; 2.3.5 Cytochrome-like Electron Transfer; 2.3.6 Stability of a Metal-Carbon Bond; 2.3.7 Metallation Reaction; 2.4 Tuning of Tetrapyrrole Structure and Function by Axial Ligands; 2.4.1 Introduction; 2.4.2 Importance of the Lower Axial Ligand for B(12) Chemistry; 2.4.3 Lower Axial Ligand in Cofactor F430; 2.4.4 Importance of Axial Ligands for the Globins; 2.4.5 Role of Axial Ligands for the Cytochromes; 2.4.6 Role of the Axial Ligand in Heme Enzymes 2.4.7 Tuning the His Ligand by Hydrogen Bonds in Heme Proteins2.4.8 Axial Ligand in Chlorophylls; 2.5 Concluding Remarks; References; 3 Modeling of Mechanisms for Metalloenzymes where Protons and Electrons Enter or Leave; 3.1 Introduction; 3.2 Energy Diagrams; 3.2.1 Photosystem II; 3.2.2 Cytochrome c Oxidase; 3.2.3 Nitric Oxide Reduction; 3.2.4 NiFe-hydrogenase; 3.2.5 Molybdenum CO Dehydrogenase; 3.3 Conclusions; References; 4 Principles of Dinitrogen Hydrogenation: Computational Insights; 4.1 Introduction 4.2 Reaction Mechanism of the Coordinated Dinitrogen Molecule in Di-zirconocene-N(2) Complexes with a Hydrogen Molecule4.2.1 Mechanism of the Reaction (3); 4.2.2 Mechanisms of the Reactions (4) and (5); 4.3 Factors Controlling the N(2) Coordination Modes in the Di-zirconocene-N(2) Complexes; 4.4 Why the [(η(5)-C(5)Me(n)H(5-n))(2)Ti](2)(μ(2),η(2),η(2)-N(2)) Complex Cannot Add a H(2) Molecule to the Side-on Coordinated N(2), while its Zr- and Hf-analogs Can 4.4.1 Relative Stability of the Lowest Singlet (S) and Triplet (T) Electronic States of the Complexes [(η(5)-C(5)Me(n)H(5-n))(2)M](2)(μ(2),η(2),η(2)-N(2)), II_M (for M = Ti, Zr, and Hf, and n = 0 and 4) |
| Altri titoli varianti | Knowledge-base for designing efficient catalysts |
| Record Nr. | UNINA-9910876767203321 |
| Weinheim, : Wiley-VCH | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||