DITHIOTHREITOL AND COBALT EFFECTS ON MEMBRANE-ASSOCIATED PEROXIDASES OXIDIZING FERULOYL-COA

K E MYTON, Stephen Fry

Research output: Contribution to journalArticlepeer-review

Abstract

Membrane preparations from cell-suspension cultures of maize produced C-14-polymeric material from [methoxy-C-14]feruloyl-CoA under conditions reported to be suitable for the assay of feruloyl-CoA: polysaccharide feruloyltransferase activity. The major C-14-polymer formed did not contain O-[C-14]feruloyl-arabinofuranosyl groups. Production of C-polymer was prevented by catalase, indicating a requirement for endogenous H2O2, and was Co2+-dependent but only in the presence of dithiothreitol (DTT). The membranes exhibited peroxidase activity with guaiacol and H2O2; this reaction was blocked by DTT. It is concluded that peroxidases and H2O2, endogenous to the isolated membranes, caused oxidative polymerization of [C-14]feruloyl groups of feruloyl-CoA; DTT prevented polymerization by acting as a competitive substrate for peroxidases, and Co2+ restored polymerization by forming an insoluble complex with the thiol.

Original languageEnglish
Pages (from-to)573-577
Number of pages5
JournalPhytochemistry
Volume38
Issue number3
Publication statusPublished - Feb 1995

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