hexacyanoferrate-iii and juglone

hexacyanoferrate-iii has been researched along with juglone* in 1 studies

Other Studies

1 other study(ies) available for hexacyanoferrate-iii and juglone

Article	Year
[Nonphysiological redox-agents are reduced at the binding center of NADP(H) glutathione reductase]. Biokhimiia (Moscow, Russia), 1992, Volume: 57, Issue:8 Studies of the acceptor reductase reaction of yeast glutathione reductase (EC 1.6.4.2) revealed that the competitive inhibitors for NADPH, 2',5'-ADP and Br- decrease the rate constants for the enzyme oxidation by ferricyanide, phenanthrene quinone, and juglone. A similar effect is observed when NADH which does not bind to the reduced enzyme is used as substrate. These observations support the hypothesis that non-physiological redox agents are reduced at the NADP(H)-binding center of glutathione reductase and that NADP(H) binding stimulates the reaction by displacing tyrosine-197 which protects FAD from the solvent. Topics: Binding Sites; Ferricyanides; Glutathione Reductase; Indicators and Reagents; NADP; Naphthoquinones; Oxidation-Reduction; Phenanthrenes; Saccharomyces cerevisiae	1992

Article

Year

[Nonphysiological redox-agents are reduced at the binding center of NADP(H) glutathione reductase].

Biokhimiia (Moscow, Russia), 1992, Volume: 57, Issue:8

Studies of the acceptor reductase reaction of yeast glutathione reductase (EC 1.6.4.2) revealed that the competitive inhibitors for NADPH, 2',5'-ADP and Br- decrease the rate constants for the enzyme oxidation by ferricyanide, phenanthrene quinone, and juglone. A similar effect is observed when NADH which does not bind to the reduced enzyme is used as substrate. These observations support the hypothesis that non-physiological redox agents are reduced at the NADP(H)-binding center of glutathione reductase and that NADP(H) binding stimulates the reaction by displacing tyrosine-197 which protects FAD from the solvent.

Topics: Binding Sites; Ferricyanides; Glutathione Reductase; Indicators and Reagents; NADP; Naphthoquinones; Oxidation-Reduction; Phenanthrenes; Saccharomyces cerevisiae

1992