Affordable Access

Artificial electron transport mediated by trinitrophenyl groups introduced into protein molecules by means of chemical modification.

Authors
Type
Published Article
Journal
Journal of biochemistry
Publication Date
Volume
96
Issue
2
Pages
371–375
Identifiers
PMID: 6094518
Source
Medline

Abstract

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.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments