Kinetic and spectral properties of pea cytosolic ascorbate peroxidase
- 1 July 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 389 (2) , 153-156
- https://doi.org/10.1016/0014-5793(96)00562-5
Abstract
Sufficient highly purified native pea cytosolic ascorbate peroxidase was obtained to characterize some of its kinetic and spectral properties. Its rate constant for compound I formation from reaction with H2O2 is 4.0 × 107 M−1 s−1, somewhat faster than is typical for peroxidases. Compound I has the typical optical spectrum of an iron(IV)‐porphyrin‐π‐cation radical, despite considerable homology with yeast cytochrome c peroxidase. The rate constant for compound I reduction by ascorbate is extremely fast (8.0 × 107 M−1 s−1 at pH 7.8), again in marked contrast to the behavior of the yeast enzyme. The pH‐rate profile for compound I formation indicates a pK a value of 5.0 for a group affecting the active site reaction.Keywords
This publication has 16 references indexed in Scilit:
- Ascorbate Peroxidase (A Prominent Membrane Protein in Oilseed Glyoxysomes)Plant Physiology, 1996
- A Novel Isoenzyme of Ascorbate Peroxidase Localized on Glyoxysomal and Leaf Peroxisomal Membranes in PumpkinPlant and Cell Physiology, 1995
- Identification of a Porphyrin .pi. Cation Radical in Ascorbate Peroxidase Compound IBiochemistry, 1995
- Crystal structure of recombinant pea cytosolic ascorbate peroxidaseBiochemistry, 1995
- Superfamily of plant, fungal and bacterial peroxidasesCurrent Opinion in Structural Biology, 1992
- Purification and Characterization of Pea Cytosolic Ascorbate PeroxidasePlant Physiology, 1991
- Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidaseFEBS Letters, 1991
- Activation of Cytoplasmic Streaming as an Adaptive Mechanism of Cultured Muskmelon Cells under Hypoxia StressPlant and Cell Physiology, 1989
- Studies on Horseradish Peroxidase. XI. On the Nature of Compounds I and II as Determined from the Kinetics of the Oxidation of FerrocyanideCanadian Journal of Chemistry, 1973
- Enthalpy of decomposition of hydrogen peroxide by catalase at 25° C (with molar extinction coefficients of H2O2 solutions in the UV)Analytical Biochemistry, 1972