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Iron Acquisition by the Genus Mycobacterium : History, Mechanisms, Role of Siderocalin, Anti-Tuberculosis Drug Development / / edited by B. Rowe Byers
Iron Acquisition by the Genus Mycobacterium : History, Mechanisms, Role of Siderocalin, Anti-Tuberculosis Drug Development / / edited by B. Rowe Byers
Edizione [1st ed. 2013.]
Pubbl/distr/stampa Cham : , : Springer International Publishing : , : Imprint : Springer, , 2013
Descrizione fisica 1 online resource (96 p.)
Disciplina 572.517
Collana SpringerBriefs in Biometals
Soggetto topico Microbiology
Proteins 
Inorganic chemistry
Bioorganic chemistry
Infectious diseases
Protein-Ligand Interactions
Inorganic Chemistry
Bioorganic Chemistry
Infectious Diseases
ISBN 3-319-00303-8
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto A History of Iron Metabolism in the Mycobacteria -- Mycobacterial Iron Uptake Mechanisms -- Siderocalin Combats Mycobacterial Infections -- Design of Anti-TB Drugs Using the Iron Uptake Platform.
Record Nr. UNINA-9910741183103321
Cham : , : Springer International Publishing : , : Imprint : Springer, , 2013
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Iron metabolism [[electronic resource] ] : from molecular mechanisms to clinical consequences / / Robert Crichton
Iron metabolism [[electronic resource] ] : from molecular mechanisms to clinical consequences / / Robert Crichton
Autore Crichton Robert R
Edizione [3rd ed.]
Pubbl/distr/stampa Chichester, UK, : John Wiley & Sons, 2009
Descrizione fisica 1 online resource (483 p.)
Disciplina 572.517
572/.5174
Soggetto topico Iron proteins
Iron - Metabolism - Disorders
Iron - Metabolism
ISBN 1-282-34583-4
9786612345838
0-470-01030-4
0-470-01029-0
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Iron Metabolism; Contents; Preface; 1. Solution Chemistry of Iron in Biological Media; 1.1 Aqueous Solution Chemistry of Iron; 1.1.1 Oxygen Free Radicals; 1.1.2 Iron Hydrolysis - a Ubiquitous Phenomenon; 1.1.3 Hydrolysis of Iron(III) in Acid Media - Formation of Polynuclear Species; 1.1.4 Ageing of Amorphous Ferrihydrite to more Crystalline Products; 1.2 Biomineralisation; 1.2.1 Magnetite Biomineralisation by Magnetotactic Bacteria; References; 2. The Importance of Iron for Biological Systems; 2.1 Introduction; 2.2 Physical Techniques for the Study of Iron in Biological Systems
2.3 Haemoproteins2.3.1 Oxygen Carriers; 2.3.2 Activators of Molecular Oxygen; 2.3.3 Electron Transport Proteins; 2.4 Iron-Sulfur Proteins; 2.5 Other Iron Containing Proteins; 2.5.1 Mononuclear Non-Haem Iron Enzymes; 2.5.2 Dinuclear Non-Haem Iron Enzymes; References; 3. Microbial Iron Transport and Metabolism; 3.1 Introduction; 3.2 Siderophores; 3.2.1 Iron Transport Across the Outer Membrane in Gram-Negative Bacteria; 3.2.2 Transport Across the Periplasm and Cytoplasmic Membrane; 3.2.3 Iron Release from Ferric Siderophores and Ferric Reduction; 3.2.4 Fe2+ Transport Systems in E. coli
3.2.5 Fe3+ Iron Acquisition by Pathogens3.3 Intracellular Iron Metabolism; 3.4 Control of Gene Expression by Iron; References; 4. Iron Uptake by Plants and Fungi; 4.1 Iron Acquisition by Plants; 4.1.1 Introduction; 4.1.2 Iron Acquisition by the Roots of Plants; 4.1.3 Long Distance Iron Transport; 4.1.4 Intracellular Iron Transport; 4.2 Iron Acquisition by Yeast; 4.2.1 Introduction - Pathways for Iron Uptake; 4.2.2 Cell Surface Reductases; 4.2.3 High Affinity Iron Transport System; 4.2.4 Low Affinity Ferrous Iron Transport; 4.2.5 Siderophore-Mediated Iron Uptake
4.2.6 Intracellular Iron Metabolism4.2.7 Iron Transport in Other Fungi; 4.2.8 Regulation of Iron Uptake/Homeostasis in Yeast; References; 5. Cellular Iron Uptake and Export in Mammals; 5.1 The Transferrins; 5.2 Structure of Transferrins; 5.3 Transferrin Iron Binding and Release; 5.4 Iron Uptake by Mammalian Cells - Uptake of Transferrin Bound Iron; 5.4.1 The Transferrin Receptor; 5.4.2 The Transferrin-to-Cell Cycle; 5.4.3 Transferrin Binding to its Receptor; 5.5 Cellular Iron Uptake and Export; 5.5.1 Red Blood Cell Precursors; 5.5.2 Tissue Macrophages; 5.5.3 Hepatocytes
5.6 Uptake of Iron from Other Sources than Transferrin5.7 Nontransferrin Bound Iron; 5.8 Ferritin Bound Iron; 5.9 Haptoglobin and Haemopexin as Iron Transporters; References; 6. Intracellular Iron Storage and Biomineralisation; 6.1 Intracellular Iron Storage; 6.1.1 Ferritin: Distribution and Primary Structure; 6.1.2 Three-Dimensional Structure; 6.1.3 The Mineral Core; 6.1.4 Iron Deposition in Ferritin; 6.1.5 Iron Mobilisation from Ferritin; 6.1.6 Haemosiderin; 6.2 Biomineralisation; References; 7. Intracellular Iron Metabolism and Cellular Iron Homeostasis; 7.1 Intracellular Iron Metabolism
7.1.1 The Labile Iron Pool
Record Nr. UNINA-9910146115403321
Crichton Robert R  
Chichester, UK, : John Wiley & Sons, 2009
Materiale a stampa
Lo trovi qui: Univ. Federico II
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Iron metabolism : inorganic biochemistry and regulatory mechanisms / / edited by Gloria C. Ferreira, José J. G. Moura, Ricardo Franco
Iron metabolism : inorganic biochemistry and regulatory mechanisms / / edited by Gloria C. Ferreira, José J. G. Moura, Ricardo Franco
Pubbl/distr/stampa Weinheim, Germany : , : Wiley-VCH, , 1999
Descrizione fisica 1 online resource (412 p.)
Disciplina 572.517
572.5174
572/.5174
Soggetto topico Iron - Metabolism
ISBN 1-281-84248-6
9786611842482
3-527-61370-6
3-527-61371-4
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Iron Metabolism; Contents; Iron Metabolism Regulation and Iron Storage; Iron and Regulation of Heme Biosynthesis; 1 Iron-dependent regulation of bacterial heme biosynthesis; 1.1 Introduction; 1.2 Summary of heme biosynthetic pathways; 1.3 Mediators of iron-dependent regulation of iron metabolism; 1.4 Regulation of heme synthesis by iron; 2 5-Aminolevulinate synthase and mammalian heme biosynthesis; 2.1 Introduction: 5-aminolevulinate synthase and iron; 2.2 Structure and mechanism: early studies; 2.2.1 Isolation, purification and identification of the PLP cofactor
2.2.2 Steady-state kinetics and mechanism of ALAS2.3 Structure and function: the active site of ALAS; 2.3.1 Identification of the Schiff base linkage between PLP and lysine-313; 2.3.2 Role of a glycine-rich loop as a PLP cofactor-binding site; 2.3.3 Role of aspartate-279 in enhancing the function of PLP and in ALAS catalysis; 2.3.4 Role of tyrosine-121 in the PLP cofactor binding; 2.3.5 Role of arginine-439 in substrate binding; 2.3.6 Active site intersubunit arrangement; 2.4 Conclusions; 3 Ferrochelatase: a new iron sulfur center-containing enzyme; 3.1 Introduction
3.2 Identification, purification and characterization of ferrochelatase3.3 Steady-state kinetic properties of ferrochelatase; 3.3.1 Ferrochelatase reaction mechanism; 3.3.2 Reducing conditions are not essential for ferrochelatase activity; 3.3.3 Site-directed mutagenesis; 3.3.4 Iron-substrate ligands as determined by Mossbauer spectroscopy; 3.4 The [2Fe-2S] cluster of mammalian ferrochelatases; 3.4.1 Conserved cysteines and iron-sulfur cluster binding; 3.4.2 Spectroscopic characterization of the [2Fe-2S] cluster; 3.5 The three-dimensional structure of Bacillus subtilis ferrochelatase
3.6 ConclusionsRegulation of Iron Transport and Metabolism; 4 The biochemistry and molecular biology of iron metabolism in yeast; 4.1 Introduction; 4.2 Iron transport in Saccharomyces cerevisiae; 4.2.2 Identification of FET3; 4.2.3 Fet3p is a multicopper oxidase; 4.2.4 Fet3p acts as a ferroxidase to mediate iron transport; 4.3 Oxidase-permease based iron transport systems in other species; 5 Role of redox-active metals in the regulation of the metallothionein and heme oxygenase genes by heme and hemopexin; 5.1 Introduction; 5.2 Hemopexin; 5.2.1 Structure; 5.3 Tissue expression of hemopexin
5.3.1 Liver5.3.2 Barrier tissues; 5.4 Heme- and heme-hemopexin-mediated effects; 5.4.1 Target tissues; 5.4.2 Responses; 5.4.2.1 Interactions between the hemopexin and transferrin systems; 5.5 Biochemical and cellular consequences of heme-hemopexin: comparison with free heme; 5.5.1 Protective role of hemopexin; 5.5.2 Increased oxidation state; 5.5.3 Transcription factors; 5.5.3.1 Redox sensitive; 5.5.3.2 For metallothionein regulation; 5.5.4 Links between iron and copper in iron homeostasis; 5.5.6 Links between heme and copper and cellular homeostasis
5.5.6.1 Role of copper in certain of the cellular and regulatory effects of hemopexin: intracellular oxidation state
Record Nr. UNINA-9910144010103321
Weinheim, Germany : , : Wiley-VCH, , 1999
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui