Artificial electron transport mediated by trinitrophenyl groups introduced into protein molecules by means of chemical modification.
Spinach ferredoxin was found to lose its iron-sulfur center during trinitrophenylation. The loss of the iron-sulfur center resulted in disappearance of its activities as electron mediators in the NADP+ photoreduction and NADPH-cytochrome c reduction systems, whereas it did not affect the activity in the cytochrome c photoreduction system. Based on the experimental evidence that ovalbumin, originally inactive in electron transport, became active in the cytochrome c photoreduction system after trinitrophenylation, the retained activity of the modified ferredoxin was concluded to be due not to the original function of the iron-sulfur center, but to artificial electron transport mediated by TNP groups introduced into the protein molecule. Trinitrophenylated cytochrome c was also active as a mediator, but lost its ability as a terminal acceptor in the system.
D000818:Animals; D002736:Chloroplasts / Q000378:metabolism; D003574:Cytochrome c Group / Q000378:metabolism*; D004579:Electron Transport / Q000187:drug effects; D005288:Ferredoxins / Q000378:metabolism*; D006736:Horses; D009206:Myocardium / Q000378:metabolism; D009578:Nitrobenzenes / Q000494:pharmacology*; D010047:Ovalbumin / Q000378:metabolism*; D010084:Oxidation-Reduction; D010788:Photosynthesis; D010944:Plants / Q000378:metabolism; D013053:Spectrophotometry; D014301:Trinitrobenzenes / Q000494:pharmacology*
D003574:Cytochrome c Group; D005288:Ferredoxins; D009578:Nitrobenzenes; D014301:Trinitrobenzenes; D010047:Ovalbumin