hexacyanoferrate-iii and 9-10-phenanthrenequinone

hexacyanoferrate-iii has been researched along with 9-10-phenanthrenequinone* in 2 studies

Other Studies

2 other study(ies) available for hexacyanoferrate-iii and 9-10-phenanthrenequinone

ArticleYear
Scanning electrochemical microscopy based evaluation of influence of pH on bioelectrochemical activity of yeast cells - Saccharomyces cerevisiae.
    Colloids and surfaces. B, Biointerfaces, 2017, Jan-01, Volume: 149

    In this research scanning electrochemical microscopy was applied for the investigation of immobilized yeast Saccharomyces cerevisiae cells. Two redox mediators based system was applied in order to increase the efficiency of charge transfer from yeast cells. 9,10-phenanthrenequinone (PQ) was applied as a lipophilic redox mediator, which has the ability to cross the cell's membrane; another redox mediator was ferricyanide, which acted as a hydrophylic electron acceptor able to transfer electrons from the PQ to the working electrode of SECM. Hill's function was applied to determine the optimal pH for this described SECM-based system. The influence of pH on cell viability could be well described by Hill's function. It was determined that at pH 6.5 the PQ has a minimal toxic influence on yeast cells, and the kinetics of metabolic processes in cells as well as electron transfer rate achieved in consecutive action of both redox mediators were appropriate to achieve optimal current signals.

    Topics: Cells, Immobilized; Electrodes; Electron Transport; Ferricyanides; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Kinetics; Microbial Viability; Microscopy, Electrochemical, Scanning; Oxidation-Reduction; Phenanthrenes; Saccharomyces cerevisiae

2017
[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