Abstract
Peroxidase associated with isolated horseradish cell walls catalyzes the formation of H2O2 in the presence of NADH. The reaction is stimulated by various monophenols, especially of coniferyl alcohol. NADH can be provided by a bound malate dehydrogenase. This system is capable of polymerizing coniferyl alcohol yielding an insoluble dehydrogenation polymer. NADH was found to be oxidized by two different mechanisms, one involving Mn2+, monophenol, and the superoxide radical O2 ·- in a reaction that is not affected by superoxide dismutase, and another one depending on the presence of free O2 ·- and probably of an enzyme-NADH complex. A scheme of these reaction chains, which are thought to be involved in the lignification process, is presented.
Similar content being viewed by others
Abbreviations
- DHP:
-
dehydrogenation polymer
- GOT:
-
glutamate oxaloacetate transaminase (EC 2.6.1.1)
- LDH:
-
lactate dehydrogenase (pig heart, EC 1.1.1.27)
- MDH:
-
malate dehydrogenase (EC 1.1.1.37)
- pCA:
-
p-coumaric acid
- SOD:
-
superoxide dismutase (EC 1.15.1.1)
- TLC:
-
thin-layer chromatography
- XOD:
-
xanthine oxidase (EC 1.2.3.2)
References
Akazawa, T., Conn, E.E.: The oxidation of reduced pyridine nucleotides by peroxidase. J. Biol. Chem. 232, 403–415 (1958)
Bielski, B.H.J., Chan, P.C.: Enzyme-catalyzed free radical reactions with nicotinamide-adenine nucleotides. I. Lactate dehydrogenase-catalyzed chain oxidation of bound NADH by superoxide radicals. Arch. Biochem. Biophys. 159, 873–879 (1973)
Elstner, E.F., Heupel, A.: On the decarboxylation of α-keto acids by isolated chloroplasts. Biochim. Biophys. Acta. 325, 182–188 (1973)
Elstner, E.F., Heupel, A.: Formation of hydrogen peroxide by isolated cell walls from horseradish (Armoracia lapathifolia Gilib.). Planta (Berl.) 130, 175–180 (1976a)
Elstner, E.F., Heupel, A.: Inhibition of nitrite formation from hydroxylammoniumchloride: A simple assay for superoxide dismutase. Anal. Biochem. 70, 616–620 (1976b)
Elstner, E.F., Konze, J.R.: Wege der Sauerstoffaktivierung in verschiedenen Kompartimenten von Pflanzenzellen. Ber. Dtsch. Bot. Ges. 89, 335–348 (1976)
Elstner, E.F., Kramer, R.: Role of the superoxide free radicalion in photosynthetic ascorbate oxidation and ascorbate-mediated photophosphorylation. Biochim. Biophys. Acta 314, 340–353 (1973)
Fridovich, I.: Oxygen radicals, hydrogen peroxide and oxygen toxicity. In: Free Radicals in Biology, vol. 1, pp. 239–277, Pryor, W.A., ed. New York-London: Academic Press 1976
Gross, G.G.: Biosynthesis of lignin and related monomers. Rec. Adv. Phytochem. 11, 141–184 (1977a)
Gross, G.G.: Cell wall-bound malate dehydrogenase from horseradish. Phytochemistry 16, 319–321 (1977b)
Gross, G.G., Jans, C.: Formation of NADH and hydrogen peroxide by cell wall-associated enzymes from Forsythia xylem. Z. Pflanzenphysiol. (1977) in press
Harkin, J.M., Obst, J.R.: Lignification in trees: Indication of exclusive peroxidase participation. Science 180, 296–298 (1973)
Kalyanaraman, V.S., Kumar, S.A., Mahadevan, S.: Oxidase-peroxidase enzymes of Datura innoxia. Oxidation of reduced nicotinamide-adenine dinucleotide in the presence of formylphenylacetic acid ethyl ester. Biochem. J. 149, 577–584 (1975)
Nimz, H., Mogharab, I., Lüdemann, H.D.: 13C-Kernresonanzspektren von Ligninen. 3. Vergleich von Fichtenlignin mit künstlichem Lignin nach Freudenberg. Z. Makromol. Chem. 175, 2563–2575 (1974)
Stafford, H.A.: Possible multienzyme complexes regulating the formation of C6-C3 phenolic compounds and lignins in higher plants. Rec. Adv. Phytochem. 8, 53–79 (1974a)
Stafford, H.A.: The metabolism of aromatic compounds. Ann. Rev. Plant Physiol. 35, 459–468 (1974b)
Whitmore, F.W.: Lignin formution in wheat coleoptile cell walls. Plant Physiol. 48, 596–602 (1971)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Gross, G.G., Janse, C. & Elstner, E.F. Involvement of malate, monophenols, and the superoxide radical in hydrogen peroxide formation by isolated cell walls from horseradish (Armoracia lapathifolia Gilib.). Planta 136, 271–276 (1977). https://doi.org/10.1007/BF00385995
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00385995