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.
- Chloroplast Cyanobacteria Enzyme modulation Fe-chelate Redox protein Thioredoxin
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
- Cell Biology