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

FEBS Letters

Juhász, András¹  Borbély, György¹  Farkas, Gábor L.¹  Udvardy, János¹ 

[1] Institute of Plant Physiology, Biological Research Center, PO Box 521, H-6701 Szeged, Hungary

关键词: Chloroplast Cyanobacteria Enzyme modulation Fe3+-chelate Redox protein Thioredoxin;    2;    6-DCPIP;    2;    6-dichlorophenolindo-phenol;    DTT;    dithiothreitol;    FBPase;    fructose-1;    6-bis-phosphatase (EC 3.1.3.11);    G6PDH;    glucose-6-phosphate dehydrogenase (EC 1.6.4.2);    NADP-GAPDH;    NADP-glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13);    NADP-MDH;    NADP-malate dehydrogenase (EC 1.1.1.12);    ICDH;    NADP-isocitrate dehydrogenase (EC 1.1.1.42);    Pi;    inorganic phosphate;    PMS;    phenazine methosulfate;    PPi;    inorganic pyrophosphate;   

DOI  :  10.1016/0014-5793(84)80862-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Fe³⁺-EDTA and the Fe³⁺ complexes of naturally occurring compounds (ATP, ADP, GTP, oxalate, pyridoxal 5'-phosphate, P_i, PP_i) 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.

【 授权许可】

Unknown