Kinetic studies on oxidation of aromatic donor molecules by horseradish peroxidase and lactoperoxidase

BioMetals

Volumn 10, Issue 1, 1997, Pages 23-26

  Modi, Sandeep ^a   Behere, Digamber V ^b  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

^b TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

Aromatic donor molecules; Horseradish peroxidase; Kinetics; Lactoperoxidase

Indexed keywords

AROMATIC COMPOUND; HEME; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; LACTOPEROXIDASE;

ARTICLE; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; OXIDATION;

ARMORACIA RUSTICANA;

EID: 0031029695     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1018310618995     Document Type: Article

References (23)

1. Bordeleau LM, Bartha R. 1972 Biochemical transformations of herbicide-derived anilines: requirements of molecular configuration. Can J Microbiol 18, 1873-1882.
2. Dunford HB, Stillman JS. 1976 Structure and functional properties of peroxidases and catalases. Coord Chem Rev 19, 187-251.
3. Frew JE, Jones P. 1984 Structure and functional properties of peroxidases and catalases. In: Sykes AG, ed. Advances in Inorganic and Bioinorganic Mechanisms. Vol. 3. London: Academic Press: 175-212.
4. Hosoya T, Fujii T, Ogawa S. 1983 A molecular orbital Study on the Oxidation of hydrogen Donor Molecules by Peroxidase Compound II. J Theor Biol 100, 283-292.
5. Hosoya T, Sakurada J, Kurokawa C, Toyada R, Nakamura S. 1989 Interaction of aromatic donor molecules with lactoperoxidase probed by optical-difference spectra. Biochemistry 28, 2639-2644.
6. Kaput J, Goltz S, Blobel G. 1982 Nucleotide-sequence of the yeast nuclear gene for cytochrome-c peroxidase precursor - functional implications of the pre sequence for protein-transport into mitochondria. J Biol Chem 257, 5054-5058.
7. Li H, Poulos TL. 1994 Structural variation in heme enzymes - A comparative-analysis of peroxidase and P450 crystal-structure. Structure 2, 461-464.
8. Modi S. 1995 Interaction of aromatic donor molecules with horseradish peroxidase: Identification of the binding site and role of heme iron in the binding and activity. Bio Metals 8, 218-222.
9. 15N nuclear magnetic resonance studies. Biochemistry 28, 4689-4694.
10. 15N nuclear magnetic resonance studies. J Biol Chem 264, 19677-19684.
11. Modi S, Behere DV, Mitra S. 1989c Binding of aromatic donor molecules to lactoperoxidase: proton NMR and optical difference spectroscopic studies. Biochim Biophys Acta 996, 214-225.
12. 15N NMR study. Biochim Biophys Acta 1038, 164-171.
13. Modi S, Behere DV, Mitra S, Bendall DS. 1991 Coordination geometry of haem in cyanogen bromide modified myoglobin and its effect on the formation of compound I. J Chem Soc (Chem Commun) 830-831.
14. 15N NMR study of the binding of thiocyanate Io chemically modified horseradish peroxidase and involvement of salt bridge. Biochim Biophys Acta 1204, 14-18.
15. Morishima I, Ogawa S. 1979 Nuclear magnetic resonance of Hemoproteins: Binding of aromatic donor molecules to horseradish peroxidase. J Biol Chem 254, 2814-2820.
16. Nichol AW, Angel LA, Moon T, Clezy PS. 1987 Lactoperoxidase heme, an iron-porphyrin thiol. Biochem J 247, 147-150.
17. Sakurada J, Takahashi S, Hosoya T. 1986 Nuclear magnetic resonance studies on the spatial relationship of aromatic donor molecules to the heme iron of horseradish peroxidase. J Biol Chem 261, 9657-9662.
18. Sakurada J, Sekiguchi R, Sato K, Hosoya T. 1990 Kinetic and molecular-orbital studies on the rate of oxidation of monosubstituted phenols and anilines by horseradish-peroxidase compound 2. Biochemistry 29, 4093-4098.
19. Saxena A, Modi S, Behere DV, Mitra S. 1990 Interaction of aromatic donor molecules with manganese(III) reconstituted horseradish peroxidase: proton NMR and optical difference spectroscopic studies. Biochim Biophys Acta 1041, 83-93.
20. Ugarova NN, Savitshi AP, Berezin IV. 1981 A Protoporphyrin-apoperoxidase Complex as a Horseradish Peroxidase Analog: A Fluorometric Study of Heme Pocket. Biochim Biophys Acta 662, 210-219.
21. Welinder KG. 1979 Amino acid Sequence Studies of Horseradish Peroxidase C: Amino and Carboxyl Termini, Cyanogen Bromide and Tryptic Fragments, the complete Sequence and some Structural Characteristics of Horseradish Peroxidase C. Eur J Biochem 96, 483-502.
22. Welinder KG. 1985 Plant peroxidases - Their primary, secondary and tertiary structures, and relation to cytochrome-c peroxidase. Eur J Biochem 151, 497-504.
23. Zeng J, Fenna RE. 1992 X-ray crystal structure of canine myeloperoxidase at 3 angstrom resolution. J Mol Biol 226, 185-207.