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[Model of bifunctional binding of rotenone and piericidin with mitochondrial NADH-dehydrogenase].

Based on authors' and literature data on the effect of inhibitors of mitochondrial NADH-dehydrogenase a scheme concerning bifunctional binding of specific inhibitors--piericidin A and rotenone with the enzyme is suggested. Analysis on the models, made in correspondence with the requirements of this scheme, permitted to propose conformations in which rotenoides interact with the enzyme.

Anti-Bacterial Agents↗
PubMed2005

[Respiration of wheat root cells under simultaneous inhibition of parts I and III of the electron transport chain of mitochondria by rotenone and antimycine A].

Respiration of excised roots of 5 day old wheat seedlings with blocked mitochondrial oxidation under simultaneous action of rotenone and antimycine A was studied. A reduced rate of oxygen uptake was observed within the first hour of root treatment inhibitors. However, after a 5 h exposure there was an increase in oxygen uptake, which was prevented by KCN but amplified by malate and ascorbate. The application of inhibitors caused a considerable increase in the respiratory coefficient (RC) up to 2.1, that suggests a significant CO2 release, when the initial sites of mitochondrial electron transport chain were inhibited. RC did not raise, when ascorbate was added in the presence of inhibitors. We assume that inhibition of mitochondrial oxidation at I and III sites of electron transport chain facilitates switching on the alternative paths of reductant translocation to oxygen. Participation of ATPases and redox system of plasma membrane in the response reactions of respiration directed to the restoration of ion, particularly, proton homeostasis in conditions of inhibited mitochondrial oxidation is discussed.

Antimycin A↗
PubMed1994

Protoporphyrin IX, an endogenous ligand of the peripheral benzodiazepine receptor, potentiates induction of the mitochondrial permeability transition and the killing of cultured hepatocytes by rotenone.

The peripheral benzodiazepine receptor (PBzR) is associated with the outer mitochondrial membrane. Protoporphyrin IX (PPIX), an endogenous substance with high affinity for the PBzR, induced the inner membrane permeability transition (MPT) in respiring liver mitochondria de-energized by carbonyl cyanide p-trifluoromethoxyphenylhydrazone. Cyclosporin A (CyA), an inhibitor of the permeability transition, prevented this effect. In cultured hepatocytes, the MPT was measured as an increased [3H]sucrose-accessible space sensitive to CyA. Nanomolar concentrations of PPIX potentiated the induction of the MPT and the extent of cell killing in hepatocyte cultures de-energized by rotenone. CyA prevented the enhanced cell killing by PPIX. PPIX did not increase the rate or extent of ATP depletion, the loss of the mitochondrial membrane potential, or the accumulation of long chain acyl-CoA thioesters. The association of the PBzR with the voltage-dependent anion channel of the outer mitochondrial membrane and with the adenine nucleotide carrier of the inner membrane suggests that this complex mediates the transport of PPIX across the mitochondrial membranes. In turn, this same complex participates in the MPT. Thus, the same structural complex (PBzR, voltage-dependent anion channel, and adenine nucleotide carrier) can interact with the endogenous substrate PPIX to result in different functional consequences depending on the state of mitochondrial energization.

Adenosine Triphosphate↗
PubMed2001

Kinetic characterization of the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae.

Saccharomyces cerevisiae mitochondria contain an NADH:Q6 oxidoreductase (internal NADH dehydrogenase) encoded by NDI1 gene in chromosome XIII. This enzyme catalyzes the transfer of electrons from NADH to ubiquinone without the translocation of protons across the membrane. From a structural point of view, the mature enzyme has a single subunit of 53 kDa with FAD as the only prosthetic group. Due to the fact that S. cerevisiae cells lack complex I, the expression of this protein is essential for cell growth under respiratory conditions. The results reported in this work show that the internal NADH dehydrogenase follows a ping-pong mechanism, with a Km for NADH of 9.4 microM and a Km for oxidized 2,6-dichorophenolindophenol (DCPIP) of 6.2 microM. NAD+, one of the products of the reaction, did not inhibit the enzyme while the other product, reduced DCPIP, inhibited the enzyme with a Ki of 11.5 microM. Two dead-end inhibitors, AMP and flavone, were used to further characterize the kinetic mechanism of the enzyme. AMP was a linear competitive inhibitor of NADH (Ki = 5.5 mM) and a linear uncompetitive inhibitor of oxidized DCPIP (Ki = 11.5 mM), in agreement with the ping-pong mechanism. On the other hand, flavone was a partial inhibitor displaying a hyperbolic uncompetitive inhibition regarding NADH, and a hyperbolic noncompetitive inhibition with respect to oxidized DCPIP. The apparent intercept inhibition constant (Kii = 5.4 microM) and the slope inhibition constant (Kis = 7.1 microM) were obtained by non linear regression analysis. The results indicate that the ternary complex F-DCPIPox-flavone catalyzes the reduction of DCPIP, although with lower efficiency. The effect of pH on Vmax was studied. The Vmax profile shows two groups with pKa values of 5.3 and 7.2 involved in the catalytic process.

2,6-Dichloroindophenol↗