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

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 tr...

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Bibliographic Details
Published in:FEBS letters 1984-06, Vol.172 (1), p.11-16
Main Authors: Udvardy, János, Borbély, György, Juhász, András, Farkas, Gábor L.
Format: Article
Language:English
Subjects:
2,6-DCPIP, 2,6-dichlorophenolindo-phenol
Biological and medical sciences
Cell structures and functions
Chloroplast Cyanobacteria Enzyme modulation Fe3+-chelate Redox protein Thioredoxin
Chloroplast, photosynthetic membrane and photosynthesis
DTT, dithiothreitol
FBPase, fructose-1,6-bis-phosphatase (EC 3.1.3.11)
Fundamental and applied biological sciences. Psychology
G6PDH, glucose-6-phosphate dehydrogenase (EC 1.6.4.2)
ICDH, NADP-isocitrate dehydrogenase (EC 1.1.1.42)
Molecular and cellular biology
NADP-GAPDH, NADP-glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13)
NADP-MDH, NADP-malate dehydrogenase (EC 1.1.1.12)
Pi, inorganic phosphate
PMS, phenazine methosulfate
PPi, inorganic pyrophosphate
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(84)80862-5