Zusammenfassung
Die Beschreibung der Struktur sowie der physiologischen Funktion von Metallzentren in Enzymen oder Proteinen hat in der bioanorganischen Chemie immer einen breiten Raum eingenommen. Zwischen der allgemein feststellbaren Häufigkeit eines Elements im Organismus (vgl. Kap. 2.1) und der spezifischen Funktion, z.B. in einem Enzym, stehen jedoch komplexe, weil notwendigerweise selektive und kontrollierte Mechanismen für Aufnahme, Transport, Speicherung und gezielte Übergabe des Elements, etwa an das dafür vorgesehene Apoprotein, unter zeitlich und räumlich genau definierten physiologischen Bedingungen. Auf diesen schwer zugänglichen Aspekt der Zeit- und Ortsabhängigkeit bioanorganischer Reaktionen im konkreten Organismus hat vor allem Williams in mehreren Artikeln hingewiesen.
“Despite their fundamental role in processes of signaling, homeostasis, and cytotoxicity little detailed information is available on the mechanisms whereby metal ions enter eukaryotic cells. Exceptions include the uptake of Fe... and the permeation of Ca2+ through Ca channels.”
D.M. Templeton J. Biot Chem. 265 (1990) 21764
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Literatur
R.J.P. Williams, Pure Appl. Chem. 55 (1983) 1089: Inorganic elements in biological space and time
R.J.P. Williams, Coord. Chem. Rev.100 (1990) 573: Bio-inorganic chemistry: Its conceptual evolution
G. Winkelmann, D. Van Der Helm, J.B. Neilands (Hrsg.): Iron Transport in Microbes, Plants and Animals, VCH, Weinheim, 1987
T.M. Loehr (Hrsg.): Iron Carriers and Iron Proteins, VCH, Weinheim, 1989
W. Schneider, Chimia 42 (1988) 9: Iron hydrolysis and the biochemistry of iron - The interplay of hydroxide and biogenic ligands
R.R. Crichton, R.J. Ward, Biochem. 31 (1992) 11255: Iron metabolism - New perspectives in view
R.R. Crichton: Inorganic Biochemistry of Iron Metabolism, Ellis Norwood, New York, 1991
B. Halliwell, J.M.C. Gurreridge, Trends Biochem. Sci. 11 (1986) 372: Iron and free radical reactions: Two aspects of antioxidant protection
E.D. Letendre, Trends Biochem. Sci. (1985) 166: The importance of iron in the pathogenesis of infection and neoplasia
N.S. Scrimshaw, Sci. Am. 265(4) (1991) 24: Iron deficiency
S. Singh, Chem. Ind. (London) (1994) 453: Therapeutically useful iron chelators
K.N. Raymond, G. Moller, B.F. Matzanke, Top. Curr. Chem. 123 (1984) 49: Cornplexation of iron by siderophores. A review of their solution and structural chemistry and biological functions
T.B. Karpishin, T.M. Dewey, K.N. Raymond, J. Am. Chem. Soc. 115 (1993) 1842: The vanadium(IV) enterobactin complex: Structural, spectroscopic, and electrochemical characterization
H. Bickel, G.E. Hall, W. Keller-Schierlein, V. Prelog, E.Vischer, A. WETTSTEIN, HeIv. Chim. Acta 43 (1960) 2129: Über die Konstitution von Fenioxamin B
F. VOGTLE: Supramolekulare Chemie, 2. Auflage, Teubner, Stuttgart, 1992
K.N. Raymond, M.E. Cass, S.L. Evans, Pure Appl. Chem. 59 (1987) 771: Metal sequestering agents in bioinorganic chemistry: Enterobactin mediated iron transport in E. coli and biomimetic applications
R.T. Reid, D.H. Live, D.J. Faulkner, A. Butler, Nature (London) 366 (1993) 455: A siderophore from a marine bacterium with an exceptional ferric ion affinity constant
Y. Mino, T. Ishida, N. OTA, M. Inoue, K. Nomoto, T. Takemoto, H. Tanaka, Y. Sugiura, J. Am. Chem. Soc. 105 (1983) 4671: Mugineic acid-iron(111) complex and its structurally analoguous cobalt(lll) complex: Characterization and implication for absorption and transport of iron in gramineous plants
B.F. Anderson, H.M. Baker, G.E. Norris D.W. Rice, E.N. Baker, J. Mol. Biol. 209 (1989) 711: Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 A resolution
E.N. Baker, Adv. lnorg. Chem. 41 (1994) 389: Structure and reactivity of transferrins
G.C. Ford, P.M. Harrison, D.W. Rice, J.M.A. Smith, A. Treffry, J.L. WHITE, J. YARN Phil. Trans. Roy. Soc. London B 304 (1984) 551: Ferritin: Design and formation of an iron-storage molecule
E.C. Theil, Annu. Rev. Biochem. 56 (1987) 289: Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms
E.C. Theil in (u), S. 259: Ferritin: A general view of the protein, the iron-protein interface, and the iron core
T.G. ST. Pierre, J. Webb, S. Mann in S. Mann, J. Webb, R.J.P. Williams (Hrsg.): Biomineralization,VCH, Weinheim, 1989: Fenitin and hemosiderin: Structural and magnetic studies of the iron core
S.J.A. Fatemi, F.H.A. Kadir, D.J. Williamson, G.R. Moore, Adv. lnorg. Chem. 36 (1991) 67: The uptake, storage, and mobilization of iron and aluminum in biology
N.D. Chasteen, C.P. Thompson, D.M. Martin in (p), S. 278: The release of iron from transfenin. An overview
J.M.A. Smith, R.F.D. Stansfield, G.C. Ford, J.L. White, P.M. Harrison in (h), Vol. 65,1988, S. 1083: A molecular model for the quartemary structure of ferritin
R.A. Eggleton, R.W. Fitzpatrick, Clays Clay Miner. 36 (1988) 111: New data and a revised structural model for ferrihydrite
K.S. Hagen, Angew. Chem. 104 (1992) 1036: Modellverbindungen für die EisenSauerstoff-Aggregation and die Biomineralisation
T.G. ST. Pierre, K.-S. Kim, J. Webb, S. Mann, D.P.E. Dickson, Inorg. Chem. 29 (1990) 1870: Biomineralization of iron: MasseauER spectroscopy and electron microscopy of ferritin cores from the chiton Acanthopleura hirtosa and the limpet Patella laticostata
R. Dagani, Chem. Eng. News, 23. November (1992) 18: Nanostructured materials promise the advance range of technologies
F. Meldrum, B.R. Heywood, S. Mann, Science 257 (1992) 522: Magnetoferritin: In vitro synthesis of a novel magnetic protein
C.M. Flynn, Chem. Rev. 84 (1984) 31: Hydrolysis of inorganic iron(Ill) salts
A.K. Powell, S.L. Heath, Comments Inorg. Chem. 15 (1994) 255: Polyiron(lll) oxyhydroxide clusters: The role of iron(Ill) hydrolysis and mineralization in nature
P.M. Harrison, G.C. Ford, D.W. Rice, J.M.A. Smith, A. Treffry, J.L. WHITE in (p), S. 268: The three-dimensional structure of apoferritin: A framework controlling ferritin ‘s iron storage and release
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2004 B. G. Teubner Verlag / GWV Fachverlage GmbH, Wiesbaden
About this chapter
Cite this chapter
Kaim, W., Schwederski, B. (2004). Aufnahme, Transport und Speicherung eines essentiellen Elements: Das Beispiel Eisen. In: Bioanorganische Chemie. Teubner Studienbücher Chemie. Vieweg+Teubner Verlag. https://doi.org/10.1007/978-3-322-92714-9_8
Download citation
DOI: https://doi.org/10.1007/978-3-322-92714-9_8
Publisher Name: Vieweg+Teubner Verlag
Print ISBN: 978-3-519-23505-7
Online ISBN: 978-3-322-92714-9
eBook Packages: Springer Book Archive