Info
- Utilizzare la checkbox di selezione a fianco di ciascun documento per attivare le funzionalità di stampa, invio email, download nei formati disponibili del (i) record.
Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
| Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Amsterdam : , : Elsevier, , 2015 |
| Descrizione fisica | 1 online resource (372 p.) |
| Collana | Advances in microbial physiology |
| Soggetto topico |
Microorganisms - Physiology
Oxygen - Physiological transport |
| Soggetto genere / forma | Electronic books. |
| ISBN |
0-12-803332-0
0-12-803298-7 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Recent Advances in Microbial Oxygen-Binding Proteins; Copyright; Contents; Contributors; Preface; Acknowledgement; Chapter One: Cytochromes cʹ: Structure, Reactivity and Relevance to Haem-Based Gas Sensing; 1. Introduction; 2. Occurrence; 3. Proposed Functional Roles of Cytochromes c'; 4. Structural Properties of Cytochromes c'; 4.1. Oligomeric State and Solvent Channels; 4.1.1. Dimer Arrangements and Monomerization; 4.1.2. Solvent Accessible Channels Between the Protein Surface and the Haem Pockets; 4.2. Haem Environment (in the Absence of Exogenous Ligands)
4.2.1. Structure of the Distal Pocket4.2.2. Structure of the Proximal Haem Pocket; 4.2.3. Redox State-Dependent Changes to the Haem Environment; 4.3. Crystal Structures of Ligand-Bound Forms; 4.3.1. Alkylisocyanide Binding to RCCP; 4.3.2. CO- and NO-Bound Structures of AXCP and SFCP; 5. Spectroscopic Properties of Cytochromes cʹ; 5.1. Haem Spectroscopy in the Absence of Exogenous Ligands; 5.1.1. Ferric Cytochromes c'; 5.1.2. Ferrous Cytochromes c'; 5.1.3. Four-Coordinate Cytochrome c'; 5.2. Haem Spectroscopy of Cytochromes cʹ with Exogenous Ligands; 5.2.1. Ferrous Complexes with NO 5.2.2. Ferrous Complexes with Carbon Monoxide5.2.3. Ferrous Complexes with Dioxygen; 5.2.4. Ferrous Complexes with Alkyl Isocyanides; 5.2.5. Ferric Complexes with Exogenous Ligands; 6. Structure-Reactivity Relationships in Cytochromes cʹ; 6.1. Distal Haem Coordination; 6.1.1. Reactivity of Cytochromes cʹ with Diatomic Gases; 6.1.1.1. Ferrous 6cXO Complexes (X=N, C, O); 6.1.1.2. Structural Determinants of Distal kon Values; 6.1.1.3. Structural Determinants of Distal koff Values; 6.1.1.4. Ligand-Induced Dimer Dissociation; 6.1.1.5. 6cNO Complexes of Ferric Cytochromes c 6.1.2. Reactivity of Cytochromes cʹ with Bulky Distal Ligands6.1.2.1. Alkyl Isocyanides; 6.1.2.2. Imidazole; 6.1.3. Reactivity of Cytochromes cʹ with Anionic Distal Ligands; 6.1.4. Conformational Control of Distal Ligand Binding in SFCP; 6.2. Proximal 5cNO Formation; 6.2.1. Determinants of Proximal 5cNO Formation; 6.2.1.1. FeHis Bond Scission; 6.2.1.2. Rapid Proximal NO Binding; 6.2.1.3. Steric Hindrance of Distal NO Binding; 6.2.1.4. Stability of the Proximal 5cNO Complex; 6.2.1.5. Long-Range Effects; 7. Relevance of Cytochrome cʹ to Other Proteins, Including Haem-Based Gas Sensors AcknowledgementsReferences; Chapter Two: Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from The...; 1. Introduction; 1.1. Microbial Haemoglobins; 1.2. Truncated Haemoglobins; 2. An Overview of Resonance Raman Spectroscopy of Haem Proteins; 2.1. Core-Size Marker Bands; 2.2. Fe-Ligand Modes; 2.2.1. The Proximal Iron-Histidine Stretching Mode; 2.2.2. The Distal Ligands; 2.2.2.1. H2O/OH-; 2.2.2.2. Fluoride; 2.2.2.3. H2S; 2.2.2.4. O2; 2.2.2.5. CO; 3. Computer Simulation Techniques; 4. Thermobifida fusca Hb; 4.1. Haem Cavity Structure 5. Spectroscopy and Computer Simulation of Tf-trHb |
| Record Nr. | UNINA-9910461009903321 |
| Amsterdam : , : Elsevier, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
| Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Amsterdam : , : Elsevier, , 2015 |
| Descrizione fisica | 1 online resource (372 p.) |
| Collana | Advances in microbial physiology |
| Soggetto topico |
Microorganisms - Physiology
Oxygen - Physiological transport |
| ISBN |
0-12-803332-0
0-12-803298-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Recent Advances in Microbial Oxygen-Binding Proteins; Copyright; Contents; Contributors; Preface; Acknowledgement; Chapter One: Cytochromes cʹ: Structure, Reactivity and Relevance to Haem-Based Gas Sensing; 1. Introduction; 2. Occurrence; 3. Proposed Functional Roles of Cytochromes c'; 4. Structural Properties of Cytochromes c'; 4.1. Oligomeric State and Solvent Channels; 4.1.1. Dimer Arrangements and Monomerization; 4.1.2. Solvent Accessible Channels Between the Protein Surface and the Haem Pockets; 4.2. Haem Environment (in the Absence of Exogenous Ligands)
4.2.1. Structure of the Distal Pocket4.2.2. Structure of the Proximal Haem Pocket; 4.2.3. Redox State-Dependent Changes to the Haem Environment; 4.3. Crystal Structures of Ligand-Bound Forms; 4.3.1. Alkylisocyanide Binding to RCCP; 4.3.2. CO- and NO-Bound Structures of AXCP and SFCP; 5. Spectroscopic Properties of Cytochromes cʹ; 5.1. Haem Spectroscopy in the Absence of Exogenous Ligands; 5.1.1. Ferric Cytochromes c'; 5.1.2. Ferrous Cytochromes c'; 5.1.3. Four-Coordinate Cytochrome c'; 5.2. Haem Spectroscopy of Cytochromes cʹ with Exogenous Ligands; 5.2.1. Ferrous Complexes with NO 5.2.2. Ferrous Complexes with Carbon Monoxide5.2.3. Ferrous Complexes with Dioxygen; 5.2.4. Ferrous Complexes with Alkyl Isocyanides; 5.2.5. Ferric Complexes with Exogenous Ligands; 6. Structure-Reactivity Relationships in Cytochromes cʹ; 6.1. Distal Haem Coordination; 6.1.1. Reactivity of Cytochromes cʹ with Diatomic Gases; 6.1.1.1. Ferrous 6cXO Complexes (X=N, C, O); 6.1.1.2. Structural Determinants of Distal kon Values; 6.1.1.3. Structural Determinants of Distal koff Values; 6.1.1.4. Ligand-Induced Dimer Dissociation; 6.1.1.5. 6cNO Complexes of Ferric Cytochromes c 6.1.2. Reactivity of Cytochromes cʹ with Bulky Distal Ligands6.1.2.1. Alkyl Isocyanides; 6.1.2.2. Imidazole; 6.1.3. Reactivity of Cytochromes cʹ with Anionic Distal Ligands; 6.1.4. Conformational Control of Distal Ligand Binding in SFCP; 6.2. Proximal 5cNO Formation; 6.2.1. Determinants of Proximal 5cNO Formation; 6.2.1.1. FeHis Bond Scission; 6.2.1.2. Rapid Proximal NO Binding; 6.2.1.3. Steric Hindrance of Distal NO Binding; 6.2.1.4. Stability of the Proximal 5cNO Complex; 6.2.1.5. Long-Range Effects; 7. Relevance of Cytochrome cʹ to Other Proteins, Including Haem-Based Gas Sensors AcknowledgementsReferences; Chapter Two: Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from The...; 1. Introduction; 1.1. Microbial Haemoglobins; 1.2. Truncated Haemoglobins; 2. An Overview of Resonance Raman Spectroscopy of Haem Proteins; 2.1. Core-Size Marker Bands; 2.2. Fe-Ligand Modes; 2.2.1. The Proximal Iron-Histidine Stretching Mode; 2.2.2. The Distal Ligands; 2.2.2.1. H2O/OH-; 2.2.2.2. Fluoride; 2.2.2.3. H2S; 2.2.2.4. O2; 2.2.2.5. CO; 3. Computer Simulation Techniques; 4. Thermobifida fusca Hb; 4.1. Haem Cavity Structure 5. Spectroscopy and Computer Simulation of Tf-trHb |
| Record Nr. | UNINA-9910797743203321 |
| Amsterdam : , : Elsevier, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK
| Recent advances in microbial oxygen-binding proteins / / [edited by] Robert K. Poole, West Riding Professor of Microbiology, Department of Molecular Biology and Biotechnology, the University of Sheffield, Firth Court, Western Bank, Sheffield, UK |
| Edizione | [First edition.] |
| Pubbl/distr/stampa | Amsterdam : , : Elsevier, , 2015 |
| Descrizione fisica | 1 online resource (372 p.) |
| Collana | Advances in microbial physiology |
| Soggetto topico |
Microorganisms - Physiology
Oxygen - Physiological transport |
| ISBN |
0-12-803332-0
0-12-803298-7 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover; Recent Advances in Microbial Oxygen-Binding Proteins; Copyright; Contents; Contributors; Preface; Acknowledgement; Chapter One: Cytochromes cʹ: Structure, Reactivity and Relevance to Haem-Based Gas Sensing; 1. Introduction; 2. Occurrence; 3. Proposed Functional Roles of Cytochromes c'; 4. Structural Properties of Cytochromes c'; 4.1. Oligomeric State and Solvent Channels; 4.1.1. Dimer Arrangements and Monomerization; 4.1.2. Solvent Accessible Channels Between the Protein Surface and the Haem Pockets; 4.2. Haem Environment (in the Absence of Exogenous Ligands)
4.2.1. Structure of the Distal Pocket4.2.2. Structure of the Proximal Haem Pocket; 4.2.3. Redox State-Dependent Changes to the Haem Environment; 4.3. Crystal Structures of Ligand-Bound Forms; 4.3.1. Alkylisocyanide Binding to RCCP; 4.3.2. CO- and NO-Bound Structures of AXCP and SFCP; 5. Spectroscopic Properties of Cytochromes cʹ; 5.1. Haem Spectroscopy in the Absence of Exogenous Ligands; 5.1.1. Ferric Cytochromes c'; 5.1.2. Ferrous Cytochromes c'; 5.1.3. Four-Coordinate Cytochrome c'; 5.2. Haem Spectroscopy of Cytochromes cʹ with Exogenous Ligands; 5.2.1. Ferrous Complexes with NO 5.2.2. Ferrous Complexes with Carbon Monoxide5.2.3. Ferrous Complexes with Dioxygen; 5.2.4. Ferrous Complexes with Alkyl Isocyanides; 5.2.5. Ferric Complexes with Exogenous Ligands; 6. Structure-Reactivity Relationships in Cytochromes cʹ; 6.1. Distal Haem Coordination; 6.1.1. Reactivity of Cytochromes cʹ with Diatomic Gases; 6.1.1.1. Ferrous 6cXO Complexes (X=N, C, O); 6.1.1.2. Structural Determinants of Distal kon Values; 6.1.1.3. Structural Determinants of Distal koff Values; 6.1.1.4. Ligand-Induced Dimer Dissociation; 6.1.1.5. 6cNO Complexes of Ferric Cytochromes c 6.1.2. Reactivity of Cytochromes cʹ with Bulky Distal Ligands6.1.2.1. Alkyl Isocyanides; 6.1.2.2. Imidazole; 6.1.3. Reactivity of Cytochromes cʹ with Anionic Distal Ligands; 6.1.4. Conformational Control of Distal Ligand Binding in SFCP; 6.2. Proximal 5cNO Formation; 6.2.1. Determinants of Proximal 5cNO Formation; 6.2.1.1. FeHis Bond Scission; 6.2.1.2. Rapid Proximal NO Binding; 6.2.1.3. Steric Hindrance of Distal NO Binding; 6.2.1.4. Stability of the Proximal 5cNO Complex; 6.2.1.5. Long-Range Effects; 7. Relevance of Cytochrome cʹ to Other Proteins, Including Haem-Based Gas Sensors AcknowledgementsReferences; Chapter Two: Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from The...; 1. Introduction; 1.1. Microbial Haemoglobins; 1.2. Truncated Haemoglobins; 2. An Overview of Resonance Raman Spectroscopy of Haem Proteins; 2.1. Core-Size Marker Bands; 2.2. Fe-Ligand Modes; 2.2.1. The Proximal Iron-Histidine Stretching Mode; 2.2.2. The Distal Ligands; 2.2.2.1. H2O/OH-; 2.2.2.2. Fluoride; 2.2.2.3. H2S; 2.2.2.4. O2; 2.2.2.5. CO; 3. Computer Simulation Techniques; 4. Thermobifida fusca Hb; 4.1. Haem Cavity Structure 5. Spectroscopy and Computer Simulation of Tf-trHb |
| Record Nr. | UNINA-9910809433103321 |
| Amsterdam : , : Elsevier, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||