Differential substrate behaviour of phenol and aniline derivatives during conversion by horseradish peroxidase

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1435, Issue 1-2, 1999, Pages 22-29

  Van Haandel, Marjon J H ^a   Claassens, Margo M J ^a   Van Der Hout, Neline ^a   Boersma, Marelle G ^a   Vervoort, J ^a   Rietjens, Ivonne M C M ^a  

^a WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Aniline; Horseradish peroxidase; Phenol; Quantitative structure activity relationship

Indexed keywords

3 METHYLANILINE; ANILINE DERIVATIVE; FERRIC ION; HORSERADISH PEROXIDASE; META CRESOL; PHENOL DERIVATIVE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME SUBSTRATE; IONIZATION; MICHAELIS MENTEN KINETICS; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; QUANTITATIVE STRUCTURE ACTIVITY RELATION;

ANILINE COMPOUNDS; BINDING SITES; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; COMPUTERS; HORSERADISH PEROXIDASE; MAGNETIC RESONANCE SPECTROSCOPY; PHENOLS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

ARMORACIA RUSTICANA; FELIS CATUS;

EID: 0032701904     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00199-5     Document Type: Article

References (23)

1. B. Chance, The Enzymes 2, part I, Academic Press, New York, 1951, pp. 428-453.
2. Dunford H.B., Stillman J.S. On the function and mechanism of action of peroxidases. Coord. Chem. Rev. 19:1976;187-251.
3. Job D., Dunford H.B. Substituent effect on the oxidation of phenols and aromatic amines by horseradish peroxidase compound I. Eur. J. Biochem. 66:1976;607-614.
4. Yamazaki I., Tamura M., Nakajima R. Horseradish peroxidase C. Mol. Cell. Biochem. 40:1981;143-153.
5. Dunford H.B., Adeniran A.J. Hammet ρσ correlation for reactions of horseradish peroxidase compound II with phenols. Arch. Biochem. Biophys. 251:1986;536-542.
6. Hosoya T., Fujii T. A molecular orbital study on the oxidation of hydrogen donor molecules by peroxidase compound II. J. Theor. Biol. 100:1983;283-292.
7. Sakurada J., Aida M., Nagata C., Hosoya T. Molecular orbital studies of the action of thyroid hormone analogs: effects on oxygen consumption of mitochondria and horseradish peroxidase-catalyzed NADH oxidation. J. Biol. Phys. 16:1988;17-23.
8. Sakurada J., Sekiguchi R., Sato K., Hosoya T. Kinetic and molecular orbital studies on the rate of oxidation of monosubstituted phenols and anilines by horseradish peroxidase compound II. Biochemistry. 29:1990;4093-4098.
9. Brewster M.E., Doerge D.R., Huang M.J., Kaminski J.J., Pop E., Bodor N. Application of semiempirical molecular orbital techniques to the study of peroxidase-mediated oxidation of phenols, anilines, sulfides and thiobenzamides. Tetrahedron. 47:1991;7525-7536.
10. van Haandel M.J.H., Rietjens I.M.C.M., Soffers A.E.M.F., Veeger C., Vervoort J., Modi S., Mondal M.S., Patel P.K., Behere D.V. Computer calculation-based quantitative structure-activity relationships for the oxidation of phenol derivatives by horseradish peroxidase compound II. J. Biol. Inorg. Chem. 1:1996;460-467.
11. Rodriguez-Lopez J.N., Smith A.T., Thorneley R.N.F. Role of arginine 38 in horseradish peroxidase. A critical residue for substrate binding and catalysis. J. Biol. Chem. 271:1996;4023-4030.
12. 1H fourier transform nuclear magnetic resonance relaxation rate studies on the interaction of acetanilide with purified isozymes of rabbit liver microsomal cytochrome P450 and with cytochrome b5. Mol. Pharmacol. 21:1982;701-709.
13. Sakurada J., Takahashi S., Hosoya T. Nuclear magnetic resonance studies on the spatial relationship of aromatic donor molecules to the heme iron of horseradish peroxidase. J. Biol. Chem. 261:1986;9657-9662.
14. P.S. Burns, R.J.P. Williams, P.E. Wright, Conformational studies of peroxidase-substrate complexes. Structure of indolepropionic acid-horseradish peroxidase complex, J. Chem. Soc. Chem. Commun. (1975) 795-796.
15. Schejter A., Lanir A., Epstein N. Binding of hydrogen donors to horseradish peroxidase: a spectroscopic study. Arch. Biochem. Biophys. 174:1976;36-44.
16. M.J.H. van Haandel, J.L. Primus, C. Teunis, M.G. Boersma, A.M. Osman, C. Veeger, I.M.C.M. Rietjens, Reversible formation of high-valent-iron-oxo porphyrin intermediates in heme-based catalysis: revisiting the kinetic model for horseradish peroxidase, Inorg. Chim. Acta 275-276 (1998) 98-105.
17. Suatoni J.C., Snyder R.E., Clark R.O. Voltammetric studies of phenol and aniline ring substitution. Anal. Chem. 33:1961;1894-1897.
18. H.B. Dunford, Horseradish peroxidase: structure and kinetic properties, in: J. Everse, K.E. Everse, M.B. Grisham (Eds.), Peroxidases in Chemistry and Biology, vol. II, CRC Press, Boca Raton, FL, 1991, pp. 1-24.
19. Patel P.K., Mondal M.S., Modi S., Behere D.V. Kinetic studies on the oxidation of phenols by horseradish peroxidase compound II. Biochim. Biophys. Acta. 1339:1997;79-87.
20. Veitch N.C. Aromatic donor molecule binding sites of haem peroxidases. Biochem. Soc. Trans. 23:1995;232-240.
21. Hendriksen A., Schuller D.J., Meno K., Welinder K.G., Smith A.T., Gajhede M. Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography. Biochemistry. 37:1998;8054-8060.
22. R.C. Weast, Handbook of Chemistry and Physics, CRC Press, Cleveland, OH, 1975.
23. Shiga T., Imaizumi K. Electron spin resonance study on peroxidase- and oxidase-reactions of horseradish peroxidase and methemoglobin. Arch. Biochem. Biophys. 167:1978;469-479.