Zusammenfassung
Drei große Gruppen eisenhaltiger Proteine lassen sich aufgrund der Ligation des Metallzentrums unterscheiden. Ausschließlich durch Aminosäurereste, Bestandteile des Wassers (H2O, HO−, O2−) oder Oxoanionen gebunden sind Eisen-Zentren im photosynthetischen Reaktionszentrum (Abbn. 4.5 - 4.7), im Hämerythrin (Kap. 5.3), in Nicht-Hämeisen-Enzymen (Kap. 7.6) und in Eisen-Transport-Proteinen (s. Kap. 8). Neben diesen oft mehrzentrigen Systemen und dem in den vorausgehenden Kapiteln 5.2 und 6 vorgestellten Porphyrinchelat-gebundenen Häm-Eisen mit seinen vielfältigen Funktionen im Sauerstoff-Metabolismus (5.8) stellen Eisen-Schwefel(Fe/S)-Zentren eine dritte große und bedeutende Klasse dar (Thomson;Salemme; Spiro; Hall, Cammack, Rao).
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Literatur
A.J. Thomson, in (o), Part 1,S. 79: Iron-Sulphur Proteins
F.R. Salemme, Annu. Rev. Biochem. 46 (1977) 299: Structure and function of cytochromes c
T.G. Spiro (Hrsg.): Iron-Sulfur Proteins, Wiley, New York, 1982
D.O. Hall, R. Cammack, K.K. Rao, Chem. Unserer Zeit 11 (1977) 165: Chemie und Biologie der Eisen-Schwefel-Proteine
B.A. Averill, W.H. Orme-Johnsonin (d), Vol. 7(1978), S. 127: Iron-sulfur proteins and synthetic analogs
A. Müller, N. Schladerbeck, Chimia 39 (1985) 23: Systematik der Bildung von Elektronentransfer-Clusterzentren (FenSnJ m + mit Relevanz zur Evolution von Ferredoxinen
R.J.P. Williams, Nature (London) 343 (1990) 213: Iron and the origin of life
K. Bosecker, Metall 34 (1980) 36: Bakterielles Leaching — Metallgewinnung mit Hilfe von Bakterien
M.S. Gebhard, J.C. Deaton, S.A. Koch, M. Millar, E.I. Solomon, J. Am. Chem. Soc. 112 (1990) 2217: Single-crystal spectral studies of Fe(SR)4 (R = 2,3,5,6-(Me) 4 C6HJ: The electronic structure of the ferric tetrathiolate active site
T. Tsukihara, K. Fukuyama, H. Tahara, Y. Katsube, Y. Matsuura, N. Tanaka, M. Kakudo, K. Wada, H. Matsubara, J. Biochem. 84 (1978) 1646: X-Ray analysis of ferredoxin from Spirulina platensis. IL Chelate structure of active center
J.A. Fee, K.L. Findling, T. Yoshida, R. Hille, G.E. Tarr, D.O. Hearshen, W.R. Dunham, E.P. Day, T.A. Kent, E. Münck, J. Biol. Chem. 259 (1984) 124: Purification and characterization of the RIESKE iron-sulfur protein from Thermus thermophilus
T.A. Link, H. Schagger, G. Von Jagow, FEBS Lett. 204 (1986) 9: Analysis of the struc-tures of the subunits of the cytochrome be I complex from beef heart mitochondria
G. Rus, B. Lamotte, J. Am. Chem. Soc. 111 (1989) 2464: Single-crystal ENDOR study of a 57 Fe-enriched iron-sulfur [Fe 4 S4 J 3 + cluster
L. Noodleman, J.G. Norman, J.H. Osborne, A. Aizman, D.A. Case, J. Am. Chem. Soc. 107 (1985) 3418: Models for ferredoxins: Electronic structures of iron-sulfur clusters with one, two, and four iron atoms
M.H. Emptage, T.A. Kent, B.H. Huynh, J. Rawlings, W.H. Orme-Johnson, E. Münck, J. Biol. Chem. 255 (1980) 1793: On the nature of the iron-sulfur centers in a ferredoxin form Azotobacter vinelandii. MOESSBAUER studies and cluster displacement experiments
G.N. George, S.J. George, Trends Biochem. Sci. 13 (1988) 369: X-ray crystallography and the spectroscopic imperative: The story of the 1. 3Fe-4S1 clusters
C.R. Kissinger, E.T. Adman, L.C. Sieker, L.H. Jensen, J. Am. Chem. Soc. 110 (1988) 8721: Structure of the 3Fe-4S cluster in Desulfovibrio gigas ferredoxin II
H. Beinert, M.C. Kennedy, Eur. J. Biochem. 186 (1989) 5: Engineering of protein bound iron-sulfur clusters
M.H. Emptage in (u), S. 343: Aconitase: Evolution of the active-site picture
S. Ciurli, M. Carrie, J.A. Weigel, M.J. Carney, T.D.P. Stack, G.C. Papaethymiou, R.H. Holm, J. Am. Chem. Soc. 112 (1990) 2654: Subsite-differentiated analogues of native [4Fe-4S1 2 +- clusters: Preparation of clusters with five-and six-coordinate subsites and modulation of redox potentials and charge distributions
T. Vagi in (q), S. 229: Hydrogenase
M.W. Adams, Biochim. Biophys. Acta 1020 (1990) 115: The structure and mechanism of iron-hydrogenases
M.S. Reynolds, R.H. Holm, Inorg. Chem. 27 (1988) 4494: Iron-sulfur-thiolate basket clusters
W.R. Hagen, A.J. Pierik, C. Veeger, J. Chem. Soc., Faraday Trans. 1 85 (1989) 4083: Novel electron paramagnetic resonance signals from an Fe/S protein containing six iron atoms
R.H. Holm, Chem. Soc. Rev. 10 (1981) 455: Metal clusters in biology: Quest for a synthetic representation of the catalytic site of nitrogenase
A. Müller, N.H. Schladerbeck, H. Bôgge, J. Chem. Soc., Chem. Commun. (1987) 35: [Fe4S4J 2-, the simplest synthetic analogue of a ferredoxin
A. Müller, N.H. Schladerbeck, Naturwissenschaften 73 (1986) 669: Einfache aerobe Bildung eines [Fe4S4J 2 + Clusterzentrums
B.A. Averill in (u): S. 258: Synthetic strategies for modeling metal-sulfur sites in proteins
T.D.P. Stack, R.H. How, J. Am. Chem. Soc. 109 (1987) 2546: Subsite-specific functionalization of the 14Fe4SJ 2 +analogue of iron-sulfur protein clusters
G. Backes, Y. Mino, T.M. Loehr, T.E. Meyer, M.A. Cusanovich, W.V. Sweeney, E.T. Adman, J. Sanders-Loehr, J. Am. Chem. Soc. 113 (1991) 2055: The environment of Fe 4 S4 clusters in ferredoxins and high-potential iron proteins. New information from X-ray crystallography and resonance Rauav spectroscopy
A. Nakamura, N. Ueyama in (u), S. 292: Importance of peptide sequence in electron-transfer reactions of iron-sulfur clusters
S.J. Lippard, Angew. Chem. 100 (1988) 353: OxoverbrÜckte Polyeisenzentren in Biologie and Chemie
J.B. Vincent, G.L. Olivier-Lilley, B.A. Averill: Chem. Rev. 90 (1990) 1447: Proteins containing oxo-bridged dinuclear iron centers: A bioinorganic perspective
M. Lammers, H. Follmann, Struct. Bonding (Berlin) 54 (1983) 27: The ribonucleotide reductases: A unique group of metalloenzymes essential for cell proliferation
A. Willing, H. Follmann, G. Auling, Eur. J. Biochem. 170 (1988) 603: Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme
P. Nordlund, B.-M. Sjoberg, H. Eklund, Nature (London) 345 (1990) 593: Three-dimensional structure of the free radical protein of ribonucleotide reductase
A. Ehrenberg in (j), S. 27: Magnetic interaction in ribonucleotide reductase
K. Wieghardt, Angew. Chem. 101 (1989) 1179: Die aktiven Zentren in manganhaltigen Metalloproteinen and anorganische Metallkomplexe
D.M. Kurtz, Chem. Rev. 90 (1990) 585: Oxo-and hydroxo-bridged diiron complexes: A chemical perspective on a biological unit
R.C. Prince, G.N. George, Trends Biochem. Sci. 15 (1990) 170: Tryptophan radicals
B.G. Fox, J.G. Bornemann, L.P. Wacketr, J.D. Lipscomb, Biochemistry 29 (1990) 6419: Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus tri-chosporium OB3b: Mechanistic and environmental implications
K. Doi, B.C. Antanan-IS, P. Aisen, Struct. Bonding (Berlin) 70 (1988) 1: The binuclear iron centers of uteroferrin and the purple acid phosphatases
S. Drüeke, K. Wieghardt, B. Nuber, J. Weiss, H.-P. Fleischhauer, S. Gehring, W. Haase, Inorg. Chem. 111 (1989) 8622: Model compounds for the oxidized uteroferrinphosphate complex
K.Schepers, B. Bremer, B. Krebs, G. Henkel, E. Althaus, B. Mosel, W. Müllerwarmuth, Angew. Chem. 102 (1990) 582: Zn(ll)Fe(Ill)- und Fe(ll)Fe(111)-Komplexe mit einer neuartigen (µ-Phenoxo)bis(µ-diphenylphosphato)dimetall(ll,lll)-Einheit als Modellkomplexe für aktive Zentren von violetten Phosphatasen
B. Krebs, G. Henkel, S. Priggemeyer, P. Eggers-Borkenstein, H. Witzel, M. Körner, D. Münstermann, H.-F. Nolting, C. Hermes in (i), S. 263: XAS investigations on purple acid phosphatases from red kidney beans and beef spleen
J.L. Beck, J. DE Jersey, B. Zerner, M.P. Hendrich, P.G. Debrunner, J. Am. Chem. Soc. 110 (1988) 3317: Properties of the Fe(11)-Fe(Ill) derivative of red kidney bean purple phosphatase. Evidence for a binuclear Zn-Fe center in the native enzyme
D.E. Wallick, L.M. Bloom, B.J. Gaffney, S.J. Benkovic, Biochemistry 23 (1984) 1295: Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron
L. Que in (h), S. 938: Spectroscopic studies of the catechol dioxygenases
L. Que in (u), S. 467: Active sites of binuclear iron-oxo proteins
D.D. Cox, L. Que, J. Am. Chem. Soc. 110 (1988) 8085: Functional models for catechol 1,2-dioxygenase. The role of the iron(111) center
C.G. Pierpont, R.M. Buchanan, Coord. Chem. Rev. 38 (1981) 44: Transition metal complexes of o-benzoquinone, o-semiquinone, and catecholate ligands
M.J. Nelson, R.A. Cowling, J. Am. Chem. Soc. 112 (1990) 2820: Observation of a peroxyl radical in samples of „purple“ lipoxygenase
M.O. Funk, R.T. Carroll, J.F. Thompson, R.H. Sands, W.R. Dunham, J. Am. Chem. Soc. 112 (1990) 5375: Role of iron in lipoxygenase catalysis
J. Stubbe, J.W. Kozarich, Chem. Rev. 87 (1987) 1107: Mechanisms of bleomycininduced DNA degradation
L.J. Ming, L. Que, A. Kriauciunas, C.A. Frolik, V.J. Chen, Inorg. Chem. 29 (1990) 1111: Coordination chemistry of the metal binding site of isopenicillin N synthase
Y. Swum, J. Kuwahara, T. Nagasawa, H. Yamada, J. Am. Chem. Soc. 109 (1987) 5848: Nitrile hydratase: The first non-heme iron enzyme with a typical low-spin Fe(III)-active center
C.J. Carrano, M.W. Carrano, K. Sharma, G. Backes, J. Sanders-Loehr, Inorg. Chem. 29 (1990) 1865: Resonance RAMAN spectra of high- and low-spin ferric phenolates. Models for dioxygenases and nitrile hydratase
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© 1991 B. G. Teubner Stuttgart
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Kaim, W., Schwederski, B. (1991). Eisen-Schwefel- und andere Nicht-Hämeisen-Proteine. In: Bioanorganishe Chemie. Teubner Studienbücher Chemie. Vieweg+Teubner Verlag, Wiesbaden. https://doi.org/10.1007/978-3-322-94722-2_7
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