Fe3+-chelates mediate the oxidative modulation of cyanobacterial and chloroplast enzymes

János Udvardy, György Borbély, András Juhász, Gábor L. Farkas

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6 Citations (Scopus)

Abstract

Fe3+-EDTA and the Fe3+ complexes of naturally occurring compounds (ATP, ADP, GTP, oxalate, pyridoxal 5'-phosphate, Pi, PPi) mediated the oxidative modulation of several, partially purified cyanobacterial and chloroplast enzymes. Cyanobacterial glucose-6-phosphate dehydrogenase deactivated by treatment with dithiothreitol + thioredoxin was reactivated in the presence of Fe3+-chelates under aerobic conditions. Cyanobacterial fructose-1,6-bisphosphatase, spinach leaf NADP-glyceraldehyde-3-phosphate dehydrogenase and NADP-malate dehydrogenase activated by incubation with dithiothreitol + thioredoxin were deactivated in the presence of Fe3+-chelates under aerobic conditions. Cyanobacterial isocitrate dehydrogenase and cyanophage AS-1-induced site-specific endonuclease, enzymes known to be devoid of redox properties, were not affected by the Fe3+ complexes. The possible role of iron-chelates in enzyme modulation is discussed.

Original languageEnglish
Pages (from-to)11-16
Number of pages6
JournalFEBS letters
Volume172
Issue number1
DOIs
Publication statusPublished - Jun 25 1984

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Keywords

  • Chloroplast Cyanobacteria Enzyme modulation Fe-chelate Redox protein Thioredoxin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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