EXAFS and XANES Studies of High-Valent Metal-Oxo Porphyrins Relevant to Horseradish Peroxidase

作者: J. E. Penner-Hahn , K. Smith Eble , J. H. Dawson , T. J. McMurry , J. T. Groves

DOI: 10.1007/978-3-642-71490-0_14

关键词:

摘要: Horseradish peroxidase is a heme-containing enzyme that catalyzes the oxidation of phenolic substrates, utilizing hydrogen peroxide as ultimate electron acceptor. The resting form HRP contains high-spin ferric heme. During catalytic cycle, initially oxidized by two electrons to green species known Compound I (HRP-I). One reduction HRP-I yields red II (HRP-II), retains one oxidizing equivalent above enzyme. There substantial interest in understanding chemistry high-valent transition metal general and peroxidases particular because their importance oxygenation reactions. In this report we review our recent EXAFS XANES studies metalloporphyrins which are relevant horseradish compounds II.

参考文章(27)
Eduardo Sarmiento P., Las fallas del mercado de capitales Revista de la CEPAL. ,vol. 1985, pp. 103- 123 ,(1985) , 10.18356/9F918C40-ES
J.E. Roberts, B.M. Hoffman, R. Rutter, L.P. Hager, Electron-nuclear double resonance of horseradish peroxidase compound I. Detection of the porphyrin pi-cation radical. Journal of Biological Chemistry. ,vol. 256, pp. 2118- 2121 ,(1981) , 10.1016/S0021-9258(19)69747-4
T L Poulos, J Kraut, B C Finzel, G C Wagner, I C Gunsalus, The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. Journal of Biological Chemistry. ,vol. 260, pp. 16122- 16130 ,(1985) , 10.1016/S0021-9258(17)36209-9
J E Hahn, K O Hodgson, L A Andersson, J H Dawson, Endogenous cysteine ligation in ferric and ferrous cytochrome P-450. Direct evidence from x-ray absorption spectroscopy. Journal of Biological Chemistry. ,vol. 257, pp. 10934- 10941 ,(1982) , 10.1016/S0021-9258(18)33913-9
G.N. La Mar, J.S. de Ropp, K.M. Smith, K.C. Langry, Proton nuclear magnetic resonance investigation of the electronic structure of compound I of horseradish peroxidase. Journal of Biological Chemistry. ,vol. 256, pp. 237- 243 ,(1981) , 10.1016/S0021-9258(19)70125-2
J E Penner-Hahn, T J McMurry, M Renner, L Latos-Grazynsky, K S Eble, I M Davis, A L Balch, J T Groves, J H Dawson, K O Hodgson, X-ray absorption spectroscopic studies of high valent iron porphyrins. Horseradish peroxidase compounds I and II and synthetic models. Journal of Biological Chemistry. ,vol. 258, pp. 12761- 12764 ,(1983) , 10.1016/S0021-9258(17)44029-4
Louise Karle Hanson, Chi K. Chang, Mary S. Davis, Jack Fajer, Electron pathways in catalase and peroxidase enzymic catalysis. Metal and macrocycle oxidations of iron porphyrins and chlorins Journal of the American Chemical Society. ,vol. 103, pp. 663- 670 ,(1981) , 10.1021/JA00393A028
Hugo Theorell, Anders Ehrenberg, Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalase Archives of Biochemistry and Biophysics. ,vol. 41, pp. 442- 461 ,(1952) , 10.1016/0003-9861(52)90473-6
Gerd N. La Mar, Jeffrey S. De Ropp, Lechoslaw Latos-Grazynski, Alan L. Balch, R. B. Johnson, Kevin M. Smith, Daniel W. Parish, Ru Jen Cheng, Proton NMR characterization of the ferryl group in model heme complexes and hemoproteins: evidence for the FeIVO group in ferryl myoglobin and compound II of horseradish peroxidase Journal of the American Chemical Society. ,vol. 105, pp. 782- 787 ,(1983) , 10.1021/JA00342A022