An investigation on the quinoprotein nature of some fungal and plant oxidoreductases

M. Maccarrone, G. A. Veldink, J. F G Vliegenthart

Research output: Contribution to journalArticle

Abstract

The presence of pyrroloquinoline quinone (PQQ) as the organic cofactor of Dactylium dendroides galactose oxidase and lentil (Lens culinaris) seedling amine oxidase, purported PQQ-containing oxidoreductases (Van der Meer, R. A., Jongejan, J. A., and Duine, J. A. (1989) J. Biol. Chem. 264, 7792-7794; Citro, G., Verdina, A., Galati, R., Floris, G., Sabatini, S., and Finazzi-Argo', A. (1989) FEBS Lett. 247, 201-204), was reinvestigated using the nitro blue tetrazolium redoxcycling method (Paz, M. A., Gallop, P. M., Torrelio, B. M., and Fluckiger, R. (1988) Biochem. Biophys. Res. Commun. 154, 1330-1337; Paz, M. A., Fluckiger, R., Boak, A., Kagan, H. M., and Gallop, P. M. (1991) J. Biol. Chem. 266, 689-692) and the enzyme-linked immunosorbent assay with polyclonal antibodies against PQQ. The possible quinoprotein nature of the laccases from Polyporus versicolor and Rhus vernicifera was also investigatged because of the similarities in spectroscopic and kinetic features of these enzymes and the laccase from Phlebia radiata, reported to be a PQQ protein (Karhunen, E., Niku-Paavola, M.-L., Viikari, L., Haltia, T., Van der Meer, R. A., and Duine, J. A. (1990) FEBS Lett. 267, 6-8). The presence of a quinonoid cofactor in lentil seedling amine oxidase is confirmed, whereas galactose oxidase and both laccases do not display any quinoprotein nature.

Original languageEnglish
Pages (from-to)21014-21017
Number of pages4
JournalJournal of Biological Chemistry
Volume266
Issue number31
Publication statusPublished - 1991

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'An investigation on the quinoprotein nature of some fungal and plant oxidoreductases'. Together they form a unique fingerprint.

  • Cite this