Zusammenfassung
Unter den vier nicht zu den Spurenelementen gerechneten Bio-Metallkationen nimmt Mg2+ aufgrund seines geringen lonenradius eine Sonderstellung ein (vgl. Tab. 13.1; Martin; Black, Huang, Cowan). Dieses Ion bevorzugt wegen des relativ kleinen Verhältnisses Radius/Ladung und der daraus folgenden Lewis-Acidität mehrfach negativ geladene Liganden, insbesondere Polyphosphate; im Gegensatz zum verwandten und in der katalytischen Funktion teilweise ähnlichen Zn2+ ist Mg2+ jedoch eindeutig ein “hartes” Elektrophil (vgl. Abb. 2.6), welches mit einfachen N- und S-Liganden wie His oder Cys− keine inerten Komplexe mehr bildet. Darüber hinaus bevorzugt Mg2+ sehr stark die Koordinationszahl sechs mit weitgehend oktaedrischer Konfiguration, während die sonst in der biologischen Funktion vergleichbaren Ionen entweder zu niedrigeren (Zn2+) oder höheren Koordinationszahlen neigen (Ca2+). Daß jedoch von dieser Regel unter dem “entatischen Streß” durch ein Enzymprotein auch abgewichen werden kann, zeigt das Beispiel der Enolase (14.9).
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.B. Martin in (d), Vil. 26 (1990), S. 1: Bioinorganic chemistry of magnesium, and following contributions
C.B. Black, H.-W. Huang, J.A. Cowan, Coord. Chem. Rev. 135/136 (1994) 165: Biological coordination chemistry of magnesium, sodium, and potassium ions
I. Andersson, S. Knight, G. Schneider, Y. Lindovist, T. Lundovist, C.-I. Branden, G.H. Lorimer, Nature (London) 337 (1989) 229: Crystal structure of the active site of ribulose-bisphosphate carboxylase
W. Hinrichs, C. Kisker, M. DÜVEL, A. MÜLLER, K. Tovar, W. Hillen, W. Saenger, Science 264 (1994) 418: Structure of the repressor-tetracycline complex and regulation of antibiotic resistance
H. Schmidbaur, H.G. Classen, J. HELBIG, Angew. Chem. 102 (1990) 1122: Asparagin-und Glutaminsäure als Liganden für Alkali-und Erdalkalimetalle: Strukturchemische Beiträge zum Fragenkomplex der Magnesiumtherapie
H. Pelletier, M.R. Sawaya, A. Kumar, S.H. Wilson, J. Kraut, Science 264 (1994) 1891: Structures of ternary complexes of rat DNA polymerase /3, a DNA template-primer, and ddCTP
A.M. Pyle, Science 261 (1993) 709: Ribozymes: A distinct class of metalloenzymes F.H. WESTHEIMER, Science 235 (1987) 1173: Why nature chose phosphates
R.B. Martin in (d), Vol. 26 (1990), S. 1: Bioinorganic chemistry of magnesium, and following contributions
J.B. Vincent, M.W. Crowder, B.A. Averill, Trends Biochem. Sci. 17 (1992) 105: Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions
L. Beese, T.A. Steitz, Embo J. 10 (1991) 25: Structural basis for the 3.-5’ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism
J. Aqvist, A. Warshel, J. Am. Chem. Soc. 112 (1990) 2860: Free energy relationships in metalloenzyme-catalyzed reactions. Calculations of the effects of metal ion substitutions in staphylococcal nuclease
A. Tsuboushi, T. Bruice, J. Am. Chem. Soc. 116 (1994) 11614: Remarkable (z1 013) rate enhancement in phosphonate ester hydrolysis catalyzed by two metal ions
H. Sigel, Coord. Chem. Rev. 100 (1990) 453: Mechanistic aspects of the metal ion promoted hydrolysis of nucleoside 5’-triphosphates
R. CINI, Comments lnorg. Chem. 13 (1992) 1: X-Ray structural studies of adenosine 5’-triphosphate metal compounds
A.S. Tracey, J. S. Jaswal, M.J. Gresser, D. Render, Inorg. Chem. 29 (1990) 4283: Condensation reactions of aqueous vanadate with the common nucleosides
D. Crans, C.D. Rithner, L.A. Theisen, J. Am. Chem. Soc. 112 (1990) 2901: Application of time-resolved 51V 2D NMR for quantitation of kinetic exchange pathways between vanadate monomer, dimer, tetramer, and pentamer
E.G. Krebs, Angew. Chem. 105 (1993) 1173: Protein-Phosphorylierung und Zellregulation I (Nobel-Vortrag)
E.H. Fischer, Angew. Chem. 105 (1993) 1181: Protein-Phosphorylierung und Zellregulation II (Nobel-Vortrag)
H.L. DE Bondt, J. Rosenblatt, J. Jancarik, H.D. Jones, D.O. Morgan, S.-H. KIM, Nature (London) 363 (1993) 595: Crystal structure of cyclin-dependent kinase 2
D.T. Lodato, G.H. Reed, Biochemistry 26 (1987) 2243: Structure of the oxalate-ATP complex with pyruvate kinase: ATP as a bridging ligand for the two divalent cations
F.J. Kayne, J. Reuben, J. Am. Chem. Soc. 92 (1970) 220: Thallium-205 nuclear magnetic resonance as a probe for studying metal ion binding to biological macromolecules. Estimate of the distance between the monovalent and divalent activators of pyruvate kinase
K.R.H. Repke, R. Schon, Biochim. Biophys. Acta 1154 (1992) 1: Chemistry and energetics of transphosphorylations on the mechanism of Na*M*-transporting ATPase: An attempt at a unifying model
L. Lebioda, B. Stec, J. Am. Chem. Soc. 111 (1989) 8511: Crystal structure of holoenolase refined at 1.9 A resolution: Trigonal-bipyramidal geometry of the cation binding site
F.L. Siegel, Struct. Bonding (Berlin) 17 (1973) 221: Calcium-binding proteins
L.J. Anghileri (Hrsg.): The Role of Calcium in Biological Systems, Vol. IV, CRC Press, Boca Raton, 1987
C. Gerday, L. Bous, R. Gilles (Hrsg.): Calcium and Calcium Binding Proteins, Springer-Verlag, Berlin, 1988
D. Pietrobon, F. Di Virgilio, T. Pozzan, Eur. J. Biochem. 193 (1990) 599: Structural and functional aspects of calcium homeostasis in eukaryotic cells
J.C. Ruegg, Naturwissenschaften 74 (1987) 579: Calcium-Regulation der Muskelkontraktion
G. Cornelius, Naturwiss. Rundschau 47 (1994) 181: Signalübertrager in der Zelle - Second-Messenger-Forschung
E. Carafoli, J.T. Penniston, Spektrum der Wissenschaften, Januar (1986) 76: Das Calcium-Signal
H. Rasmussen, Spektrum der Wissenschaften, Dezember (1989) 128: Der Membrankreislauf von Calcium als intrazelluläres Signal
S. Klumpp, J.E. Schultz, Pharm. Unserer Zeit 14 (1983) 19: Calcium und Calmodulin D.M.E. SZEBENYI, K. MOFFAT, J. Biol. Chem. 261 (1986) 8761: The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine
S. Goldmann, J. Stoltefuss, Angew. Chem. 103 (1991) 1587: 1,4-Dihydropyridine: Einfluss von Chiralität und Konformation auf die Calcium-antagonistische und -agonistische Wirkung
R. Fossheim, K. Svarteng, A. Mostad, C. Romming, E. Shefter, D.J. TRIGGLE, J. Med. Chem. 25 (1982) 126: Crystal structures and pharmacological activity of calcium channel antagonists
O. Bachs, N. Agell, E. Carafoli, Biochim. Biophys. Acta 1113 (1992) 259: Calcium and calmodulin function in the cell nucleus
E. Carafoli, Faseb J. 8 (1994) 993: Biogenesis: Plasma membrane calcium ATPase: 15 years of work on the purified enzyme
R.Y. Tsien, Chem. Eng. News July 18 (1994) 34: Fluorescence imaging creates a window on the cell
M. Ochsner-Bruderer, T. Fleck, Nachr. Chem. Tech. Lab. 41 (1993) 997: Fluori-metrische Bestimmung der intrazellulären Calciumionen-Konzentration
T. Hirano, I. Mizoguchi, M. Yamaguchi, F.-Q. Chen, M. Ohashi, Y. Ohmiya, F.I. Tsuji, J. Chem. Soc., Chem. Commun. (1994) 165: Revision of the structure of the light-emitter in aequorin bioluminescence
A.M. Albrecht-Gary, S. Blanc-Parasote, D.W. BOYD, G. Dauphin, G. Jeminet, J. Juillard, M. Prudhomme, C. Tissier, J. Am. Chem. Soc. 111 (1989) 8598: X-14885A: An ionophore closely related to calcimycin (A-23187). NMR, thermodynamic, and kinetic studies of cation selectivity
Y. Ogoma, T. Shimizu, M. Hatano, T. Fuji!, A. Hachimori, Y. Kondo, Inorg. Chem. 27 (1988) 1853: 43 Ca nuclear magnetic resonance spectra of Ca 2 +-S100 protein solutions
A.L. Swain, E.L. Amma, Inorg. Chim. Acta 163 (1989) 5: The coordination polyhedron of Ca 2+ Cd 2+ in parvalbumin
N.K. Vyas, M.N. Vyas, F.A. Quiocho, Nature (London) 327 (1987) 635: A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
K.A. Satyshur, S.T. RAO, D. Pyzalska, W. Drendel, M. GREASER, M. SUNDARALINGAM, J. Biol. Chem. 263 (1988) 1628: Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution
P. Chakrabarti, Biochemistry 29 (1990) 651: Systematics in the interaction of metal ions with the main-chain carbonyl group in protein structures
W.I. Weis, K. Drickamer, W.A. Hendrickson, Nature (London) 360 (1992) 127: Structure of a C-type mannose-binding protein complexed with an oligosaccharide
M. Ohnishi, R.A.F. Reithmeier, Biochemistry 26 (1987) 7458: Fragmentation of rabbit skeletal muscle calsequestrin: Spectral and ion binding properties of the carboxyl-terminal region
P.J. Mclaughlin, J.T. GOOCH, H.G. Mannherz, A.G. Weeds, Nature (London) 364 (1993) 685: Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
F.A. Corrow, E.E. Hazen, M.J. Legg, Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 2551: Staphylococcal nuclease: Proposed mechanism of action based on structure of enzyme-thymidine 3’,5’-bisphosphate-calcium ion complex at 1.5-A resolution
A. S. Babu, J.S. Sack, T.J. Greenhough, C.E. Bugg, A.R. Means, W.J. COOK, Nature (London) 315 (1985) 37: Three-dimensional structure of calmodulin
S. Forsen, J. Kordel, Acc. Chem. Res. 26 (1993) 7: The molecular anatomy of a calcium-binding protein
W.E. Meador, A.R. Means, F.A. Quiocho, Science 257 (1992) 1251: Target enzyme recognition by calmodulin: 2.4 A Structure of a calmodulin-peptide complex
D. Kligman, D.C. Hilt, Trends Biochem. Sci. 13 (1988) 437: The S100 protein family P. DEMANGE, D. VOGES, J. BENZ, S. LIEMANN, P. GOTrIG, R. BERENDES, A. BURGER, R. HUBER, Trends Biol. Sci. 19 (1994) 272: Annexin V: The key to understanding ion selctivity and voltage regulation?
E.I. Ochiai, J. Chem. Educ. 68 (1991) 10: Why calcium?
C.H. EVANS, Trends Biochem. Sci. (1983) 445: Interesting and useful biochemical properties of lanthanides
K. Fujimori, M. Sorenson, O. HERZBERG, J. MOULT, F.C. Reinach, Nature (London) 345 (1990) 182: Probing the calcium-induced conformational transition of troponin C with site-directed mutants
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). Katalyse und Regulation bioenergetischer Prozesse durch die Erdalkalimetallionen Mg2+ und Ca2+ . In: Bioanorganische Chemie. Teubner Studienbücher Chemie. Vieweg+Teubner Verlag. https://doi.org/10.1007/978-3-322-92714-9_14
Download citation
DOI: https://doi.org/10.1007/978-3-322-92714-9_14
Publisher Name: Vieweg+Teubner Verlag
Print ISBN: 978-3-519-23505-7
Online ISBN: 978-3-322-92714-9
eBook Packages: Springer Book Archive