LEADER 05222nam 2200625 450 001 9910144010103321 005 20230422044845.0 010 $a1-281-84248-6 010 $a9786611842482 010 $a3-527-61370-6 010 $a3-527-61371-4 035 $a(CKB)1000000000376031 035 $a(EBL)481320 035 $a(SSID)ssj0000183820 035 $a(PQKBManifestationID)11170428 035 $a(PQKBTitleCode)TC0000183820 035 $a(PQKBWorkID)10199687 035 $a(PQKB)10097173 035 $a(MiAaPQ)EBC481320 035 $a(OCoLC)212131900 035 $a(EXLCZ)991000000000376031 100 $a20160818h19991999 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aIron metabolism $einorganic biochemistry and regulatory mechanisms /$fedited by Gloria C. Ferreira, Jose? J. G. Moura, Ricardo Franco 210 1$aWeinheim, Germany :$cWiley-VCH,$d1999. 210 4$dİ1999 215 $a1 online resource (412 p.) 300 $aIncludes index. 311 $a3-527-29653-0 327 $aIron 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 327 $a2.2.2 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 327 $a3.2 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 327 $a3.6 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 327 $a5.3.1 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 327 $a5.5.6.1 Role of copper in certain of the cellular and regulatory effects of hemopexin: intracellular oxidation state 330 $aIron 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 606 $aIron$xMetabolism 615 0$aIron$xMetabolism. 676 $a572.517 676 $a572.5174 676 $a572/.5174 702 $aFerreira$b Glo?ria C. 702 $aMoura$b Jose? J. G. 702 $aFranco$b Ricardo 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910144010103321 996 $aIron Metabolism$9834677 997 $aUNINA