05222nam 2200625 450 991014401010332120230422044845.01-281-84248-697866118424823-527-61370-63-527-61371-4(CKB)1000000000376031(EBL)481320(SSID)ssj0000183820(PQKBManifestationID)11170428(PQKBTitleCode)TC0000183820(PQKBWorkID)10199687(PQKB)10097173(MiAaPQ)EBC481320(OCoLC)212131900(EXLCZ)99100000000037603120160818h19991999 uy 0engur|n|---|||||txtccrIron metabolism inorganic biochemistry and regulatory mechanisms /edited by Gloria C. Ferreira, José J. G. Moura, Ricardo FrancoWeinheim, Germany :Wiley-VCH,1999.©19991 online resource (412 p.)Includes index.3-527-29653-0 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 cofactor2.2.2 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 Introduction3.2 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 ferrochelatase3.6 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 hemopexin5.3.1 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 homeostasis5.5.6.1 Role of copper in certain of the cellular and regulatory effects of hemopexin: intracellular oxidation stateIron plays a crucial role in many biochemical processes. In recent years intensive research has led to a better understanding of the function of iron in cellular metabolism. In more than twenty articles internationally renowned experts give a thorough account of the recent developments of this fascinating field. The book focuses on the central questions, e.g. transport, storage, and utilization of iron in cells, the three-dimensional structure of iron-containing proteins, the physiological function of heme and iron sulfur-containing proteins, and the regulatory mechanisms in heme biosynthesis IronMetabolismIronMetabolism.572.517572.5174572/.5174Ferreira Glória C.Moura José J. G.Franco RicardoMiAaPQMiAaPQMiAaPQBOOK9910144010103321Iron Metabolism834677UNINA02058oam 2200589 450 991070658480332120171116090706.0(CKB)5470000002456596(OCoLC)891600304(OCoLC)995470000002456596(EXLCZ)99547000000245659620140929d1963 ua 0engurmn|||||||||txtrdacontentcrdamediacrrdacarrierAn aeromagnetic reconnaissance of the Cook Inlet area, Alaska /by Arthur Grantz, Isidore Zietz, and Gordon E. AndreasenWashington :United States Department of the Interior, Geological Survey,1963.1 online resource (22 unnumbered pages) illustrations, maps +5 platesGeological Survey professional paper ;316-GGeophysical field investigationsTitle from title screen (viewed September 26, 2014)."A regional geologic interpretation of the magnetic field over the Cook Inlet."Includes bibliographical references (page 134).Aeronautics in geologyGeologyAlaskaCook InletGeomagnetismAlaskaCook InletAeronautics in geologyfastGeologyfastGeomagnetismfastCook Inlet (Alaska)Pacific OceanCook InletfastAeronautics in geology.GeologyGeomagnetismAeronautics in geology.Geology.Geomagnetism.Grantz Arthur1927-2021,1276837Zietz Isidore1919-Andreasen Gordon E.1924-Geological Survey (U.S.),COPCOPOCLCOOCLCFGPOBOOK9910706584803321An aeromagnetic reconnaissance of the Cook Inlet area, Alaska3522573UNINA