Biopolym. Cell. 2003; 19(1):31-36.
Structure and Function of Biopolymers
Kinetic properties of the Penicilium vitale catalase. Catalytic reaction of the enzyme
1Gudkova L. V., 1Latyshko N. V., 1Gudkova O. A.
  1. Palladin Institute of Biochemistry, NAS of Ukraine
    9, Leontovycha Str., Kyiv, Ukraine, 01601


The fast kinetics of the P. vitale catalase (CPV) catalytic reaction was investigated by the stop-flow technique. The transient-state rate constants of the intermediate complex (Compound I) formation as well as the rate of spontaneous dissociation and dissociation resulting in the reaction product creation were found at 25 °C to be 0.614·106 M-1s-1, 1.78 s-1 and 1.85·106 M-1s-1, respectively.


[1] Latyshko NV, Gudkova LV. The kinetic and catalytic properties of Penicillium vitale catalase. Ukr Biokhim Zh. 1996;68(2):69-73.
[2] Latyshko NV, Gudkova LV, Gudkova OA. Catalytic properties of the Penicilium vitate catalase. Peroxidatic reaction of the enzyme. Biopolym Cell. 2000; 16(6):505-9.
[3] Du P, Loew GH. Theoretical study of model compound I complexes of horseradish peroxidase and catalase. Biophys J. 1995;68(1):69-80.
[4] Adachi S, Nagano S, Ishimori K, Watanabe Y, Morishima I, Egawa T, Kitagawa T, Makino R. Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase. Biochemistry. 1993;32(1):241-52.
[5] Dounce AL, Sichak SP. Hematin iron valence in catalase and peroxidase compound I: relationship to free radical reaction mechanism. Free Radic Biol Med. 1988;5(2):89-93.
[6] Rodr?guez Mara??n MJ, Mercier D, van Huystee RB, Stillman MJ. Analysis of the optical absorption and magnetic-circular-dichroism spectra of peanut peroxidase: electronic structure of a peroxidase with biochemical properties similar to those of horseradish peroxidase. Biochem J. 1994;301 ( Pt 2):335-41.
[7] Bursey EH, Poulos TL. Two substrate binding sites in ascorbate peroxidase: the role of arginine 172. Biochemistry. 2000;39(25):7374-9.
[8] Palcic MM, Dunford HB. The reaction of human erythrocyte catalase with hydroperoxides to form compound I. J Biol Chem. 1980;255(13):6128-32.
[9] Noble RW, Gibson QH. The reaction of ferrous horseradish peroxidase with hydrogen peroxide. J Biol Chem. 1970;245(9):2409-13.
[10] Keilin D, Nicholls P. Reactions of catalase with hydrogen peroxide and hydrogen donors. Biochim Biophys Acta. 1958;29(2):302-7.
[11] Oshino N, Chance B, Sies H. The properties of the secondary catalase—peroxide complex (Compound II) in the hemoglobin-free perfused rat liver. Arch Biochem Biophys. 1973;159(2):704-11.
[12] Nicholls P. The formation and catalytic role of catalase peroxide compound II. Biochim Biophys Acta. 1964;81:479-95.
[13] Strickland S, Palmer G, Massey V. Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data. J Biol Chem. 1975;250(11):4048-52.
[14] Chance B, Greenstein DS, Higgins J, Yang CC. The mechanism of catalase action. II. Electric analog computer studies. Arch Biochem Biophys. 1952;37(2):322-39.
[15] Clayton RK. Purified catalase from Rhodopseudomonas spheroides. Biochim Biophys Acta. 1959;36:40-7.
[16] Chance B, Oshino N. Kinetics and mechanisms of catalase in peroxisomes of the mitochondrial fraction. Biochem J. 1971;122(2):225-33.
[17] Deisseroth A, Dounce AL. Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role. Physiol Rev. 1970;50(3):319-75.
[18] Zidoni E, Kremer ML. Kinetics and mechanism of catalase action. Formation of the intermediate complex. Arch Biochem Biophys. 1974;161(2):658-64.
[19] Wariishi H, Dunford HB, MacDonald ID, Gold MH. Manganese peroxidase from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Transient state kinetics and reaction mechanism. J Biol Chem. 1989;264(6):3335-40.
[20] Jones P, Suggett A. The catalase-hydrogen peroxide system. A theoretical appraisal of the mechanism of catalase action. Biochem J. 1968;110(4):621-9.
[21] Kozlov EA, Levitina TL, Bobrovskaia MT, Gudkova LV, Latyshko NV, Radomski? NF. Complete amino acid sequence of catalase from the fungus Penicillium vitale. Bioorg Khim. 1998;24(3):163-70.