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Katalyse durch Hämoproteine: Elektronenübertragung, Sauerstoffaktivierung und Metabolismus anorganischer Zwischenprodukte

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Bioanorganische Chemie

Part of the book series: Teubner Studienbücher Chemie ((TSBC))

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Zusammenfassung

Eisenporphyrin-Komplexe besitzen neben der Fähigkeit zum stöchiometrischen Disauerstoff-Transport vielfältige katalytische Funktionen im biochemischen Geschehen. Neben dem eigentlichen Häm-System (5.8) kommen auch Eisenkomplexe mit teilreduzierten Porphyrinliganden wie etwa Chlorin (→ Häm d) oder Sirohäm vor (vgl. 6.20). Häm-enthaftende Enzyme sind an Elektronentransport und -akkumulation, an der kontrollierten Umsetzung sauerstoffhaltiger Zwischenprodukte wie etwa O 2−2 , NO −2 oder SO 2−3 sowie zusammen mit anderen prosthetischen Gruppen an komplexen Redoxprozessen beteiligt (vgl. die Cytochrom c-Oxidase, Kap. 10.4).

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Literatur

  • G. VON Jagow, W.D. Engel, Angew. Chem. 92 (1980) 684: Struktur und Funktion des energieumwandelnden Systems der Mitochondrien

    Google Scholar 

  • C. Greenwood in (o), Teil 1S. 43: Cytochromes c and cytochrome c containing enzymes

    Google Scholar 

  • G.R. Moore, G.W. Pettigrew:Cytochromes cSpringer-Verlag, Berlin, 1990

    Google Scholar 

  • G. Palmer, J. Reedijk, Eur. J. Biochem. 200 (1991) 599: Nomenclature of electron-transfer proteins

    Google Scholar 

  • G.N. George, T. Richards, R.E. Bare, Y. Gea, R.C. Prince, E.I. Stiefel, G.D. Watts, J. Am. Chem. Soc. 115 (1993) 7716: Direct observation of bis-sulfur ligation to the heme of bacterioferritin

    Google Scholar 

  • F.R. Salemme, Annu. Rev. Biochem. 46 (1977) 299: Structure and function of cytochromes c

    Google Scholar 

  • R.J.P. Williams in M.K. Johnson et al. (Hrsg.): Electron Transfer in Biology,Adv. Chem. Ser. 226 (1990), S. 3: Overview of biological electron transfer

    Google Scholar 

  • H.B. Gray, B.G. Malmstrom, Biochemistry 28 (1989) 7499: Long-range electron transfer in multisite metalloproteins

    Google Scholar 

  • J.R. Miller, Nouv. J. Chim. 11 (1987) 83: Controlling charge separation through effects of energy distance and molecular structure on electron transfer rates

    Google Scholar 

  • R.C. Prince, G.N. George, Trends Biochem. Sci. 15 (1990) 170: Tryptophan radicals T.L. PouLOs in (c), Vol. 7 (1988) 1: Herne enzyme crystal structures

    Google Scholar 

  • H. Pelletier, J. KRAUT, Science 258 (1992) 1748: Crystal structure of a complex between electron transfer partners cytochrome c peroxidase and cytochrome c

    Google Scholar 

  • J. Deisenhofer, H. Michel, Angew. Chem. 101 (1989) 872: Das photosynthetische Reaktionszentrum des Purpurbakteriums Rhodopseudomonas viridis (Nobel-Vortrag)

    Google Scholar 

  • W.R. Scheidt, C.A. Reed, Chem. Rev. 81 (1981) 543: Spin-state/stereochemical relationships in iron porphyrins: Implications for the hemoproteins

    Google Scholar 

  • S.G. Sligar, K.D. Egeberg, J.T. Sage, D. Morikis, P.M. Champion, J. Am. Chem. Soc. 109 (1987) 7896: Alteration of heme axial ligands by site-directed mutagenesis: A cytochrome becomes a catalytic demethylase

    Google Scholar 

  • P.R. Ortiz De Montellano, Acc. Chem. Res. 20 (1987) 289: Control of the catalytic activity of prosthetic heme by the structure of hemoproteins

    Google Scholar 

  • F.P. Guengerich, J. Biol. Chem. 266 (1991) 10019: Reactions and significance of cytochrome P-450 enzymes

    Google Scholar 

  • T.D. Porter, M.H. Coon, J. Biol. Chem. 266 (1991) 13469: Cytochrome P-450

    Google Scholar 

  • K. Ruckpaul, Pharm. Unserer Zeit 22 (1993) 296: Cytochrome P-450 abhängige Enzyme

    Google Scholar 

  • D. Mansuy, Pure Appl. Chem. 66 (1994) 737: Cytochromes P-450 and model systems: Great diversity of catalyzed reactions

    Google Scholar 

  • W.B.Jakoby, D. M. Ziegler, J. Biol. Chem. 265 (1990) 20715: The enzymes of detoxification

    Google Scholar 

  • G. Fellenberg:Chemie der Umweltbelastung2. Aufl., Teubner, Stuttgart, 1992

    Google Scholar 

  • D. Lenoir, H. Sandermann, JR., Biol. Unserer Zeit 23 (1993) 363: Entstehung und Wirkung von Dioxinen

    Google Scholar 

  • E. Mutschler:Arzneimittelwirkungen Lehrbuch der Pharmakologie und Toxikologie6. Aufl., WVG, Stuttgart, 1991

    Google Scholar 

  • H. Patzelt, W.D. Woggon, HeIv. Chim. Acta 75 (1992) 523: O-Insertion into nonactivated C-H bonds: The first observation of 0 2 cleavage by a P-450 enzyme model in the presence of a thiolate ligand

    Google Scholar 

  • R. Raag, T.L. Poulos, Biochemistry 28 (1989) 917: The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM

    Google Scholar 

  • K.G. Ravichandran, S.S. Boddupalli, C.A. Hasemann, J.A. Peterson, J. Deisenhofer, Science 261 (1993) 731: Crystal structure of hemoprotein domain of P450BM-3 a prototype for microsomal P450’s

    Google Scholar 

  • N.C. Gerber, S.G. Sligar, J. Am. Chem. Soc. 114 (1992) 8742: Catalytic mechanism of cytochrome P-450: Evidence for a distal charge relay

    Google Scholar 

  • D. Mandon, R. Weiss, M. Franke, E. Bill, A.X. Trautwein, Angew. Chem. 101 (1989) 1747: Ein Oxoeisenporphyrinat mit höhenwertigem Eisen: Bildung durch lösungsmittelabhängige Protonierung eines Peroxoeisen(111)-porphyrinat-Derivats

    Google Scholar 

  • J.T. Groves, Y. Watanabe, J. Am. Chem. Soc. 110 (1988) 8443: Reactive iron por-phyrin derivatives related to the catalytic cycles of cytochrome P-450 and peroxidase

    Google Scholar 

  • K.L. Kostka, B.G. Fox, M.P. Hendrich, T.J. Collins, C.E.F. Richard, L.J. Wright, E. Münck, J. Am. Chem. Soc. 115 (1993) 6746: High-valent transition metal chemistry. Mössbauer and EPR studies of high-spin (S=2) iron(IV) and intermediate-spin (S=3/2) iron(Ill) complexes with a macrocyclic tetraamido-N ligand

    Google Scholar 

  • D.T. Sawyer, Comments Inorg. Chem. 6 (1987) 103: The nature of the bonding and valency for oxygen in its metal compounds

    Google Scholar 

  • P.M. Champion, J. Am. Chem. Soc. 111 (1989) 3433: Elementary electronic excitations and the mechanism of cytochrome P450

    Google Scholar 

  • W.A. Herrmann, J. Organomet. Chem. 300 (1986) 111: Zufallsentdeckung am Beispiel Rhenium: Oxo-Komplexe in hohen und niedrigen Oxidationsstufen

    Google Scholar 

  • J. Everse, K.E. Everse, M.B. Grisham (Hrsg.): Peroxidases in Chemistry and Biology, Vol. 2, CRC Press, Boca Raton, 1990

    Google Scholar 

  • T. Haag, F. Lingens, K.-H. VAN Pee, Angew. Chem. 103 (1991) 1550: Eine Metall-Ionen und Cofaktor-unabhängige enzymatische Redoxreaktion: die Halogenierung durch bakterielle Nicht-Häm-Haloperoxidasen

    Google Scholar 

  • S. Hashimoto, R. Nakajima, I. Yamazaki, T. Kotani, S. Ohtaki, T. Kitagawa, FEBS Lett. 248 (205) 1989: Resonance RAMAN characterization of hog thyroid peroxidase

    Google Scholar 

  • H.E. Schoemaker, Red. Tray. Chim. Pays-Bas 109 (1990) 255: On the chemistry of lignin biodegradation

    Google Scholar 

  • J.H. Dawson, Science 240 (1988) 433: Probing structure-function relations in hemecontaining oxygenases and peroxidases

    Google Scholar 

  • K. Yamaguchi, Y Watanabe, I. Morishima, J. Am. Chem. Soc. 115 (1993) 4058: Direct observation of the push effect on the O-O bond cleavage of acylperoxoiron(lll) porphyrin complexes

    Google Scholar 

  • M.G. Peter, Angew. Chem. 101 (1989) 572: Chemische Modifikation von Biopolymeren durch Chinone und Chinonmethide

    Google Scholar 

  • K.E. Hammel in (d), Vol. 28 (1992), S. 41: Oxidation of aromatic pollutants by lignin-degrading fungi and their extracellular peroxidases

    Google Scholar 

  • G. Winkelmann (Hrsg.): Microbial Degradation of Natural Products, VCH Publishers, New York, 1992

    Google Scholar 

  • P.M.H. Kroneck, J. Beuerle, W. Schumacher in (d) Vol. 28 (1992), S. 455: Metal-dependent conversion of inorganic nitrogen and sulfur compounds

    Google Scholar 

  • T. Brittain, R. Blackmore, C. Greenwood, A.J. Thomson Eur. J. Biochem. 209 (1992) 793: Bacterial nitrite-reducing enzymes

    Google Scholar 

  • M.J. Clarke, J.B. Gaul, Struct. Bonding (Berlin), 81 (1993) 147: Chemistry relevant to the biological effects of nitric oxide and metallonitrosyls

    Google Scholar 

  • U. Forstermann, Biol. Unserer Zeit 24 (1994) 62: Stickoxid (NO): Umweltgift und körpereigener Botenstoff

    Google Scholar 

  • J.S. Stamler, D.J. Singel, J. LoscALzo, Science 258 (1992) 1898: Biochemistry of nitric oxide and its redox-activated forms

    Google Scholar 

  • E.Culotta, D.E. Koshland, Science 258 (1992) 1862: NO news is good news

    Google Scholar 

  • F. Murad, Angew. Chem. 111 (1999) 1953: Die Entdeckung einiger biologischer Wirkungen von Stickstoffmonoxid und seine Rolle für die Zeltkommunikation

    Google Scholar 

  • R.F. Furchgott, Angew. Chem. 111 (1999) 1990: Der relaxierende Faktor aus Endothelzellen: Entdeckung, frühe Untersuchungen und Identifizierung als Stickstoffmonoxid

    Google Scholar 

  • L.J. Ignarro, Angew. Chem. 111 (1999) 2002: Stickstoffmonoxid: ein einzigartiges endogenes Signalmolekül in der Gefäßbiologie

    Google Scholar 

  • A.L. Burnett, C.J. Lowenstein, D.S. Bredt, T.S.K. Chang, S.H. Snyder, Science 257 (1992) 401: Nitric oxide: A physiologic mediator of penile erection

    Google Scholar 

  • M.A. Marletta, J. Biol. Chem. 268 (1993) 12231: Nitric oxide synthase structure and mechanism

    Google Scholar 

  • A. Verma, D.J. Hirsch, C.E. Glatr, G.V. Ronnett, S.H. Snyder, Science 259 (1993) 381: Carbon monoxide. A putative neural messenger?

    Google Scholar 

  • C.K. Chang, R. Timkovich, W. Wu, Biochemistry 25 (1986) 8447: Evidence that heme dl is a 13-porphyrindione

    Google Scholar 

  • M.P. Hendrich, M. Logan, K.K. Andersson, D.M. Arciero, J.D. Lipscomb, A.B. Hooper, J. Am. Chem. Soc. 116 (1994) 11961: The active site of hydroxylamine oxidoreductase from Nitrosomonas: Evidence for a new metal cluster in enzymes

    Google Scholar 

  • H. Tributsch, J. Electroanal. Chem. 331 (1992) 783: On the significance of the simultaneity of electron transfer and cooperation in electrochemistry

    Google Scholar 

  • D.E. Mcree, D.C. Richardson, J.S. Richardson, L.M. Siegel, J. Biol. Chem. 261 (1986) 10277: The heme and Fe 4 S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase

    Google Scholar 

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Authors
  1. Prof. Dr. phil. nat. Wolfgang Kaim
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  2. Dr. rer. nat. Brigitte Schwederski
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Kaim, W., Schwederski, B. (2005). Katalyse durch Hämoproteine: Elektronenübertragung, Sauerstoffaktivierung und Metabolismus anorganischer Zwischenprodukte. In: Bioanorganische Chemie. Teubner Studienbücher Chemie. Vieweg+Teubner Verlag, Wiesbaden. https://doi.org/10.1007/978-3-663-01605-2_6

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