ubiquinol and plastoquinol

Many mitochondria-targeted antioxidants (MTAs) that comprise a quinol moiety covalently attached through an aliphatic carbon chain to the lipophilic triphenylphosphonium cation are widely used for evaluating the role of mitochondria in pathological processes involving oxidative stress. The potency of MTAs to carry electrons across biological membranes and thereby mediate transmembrane redox processes was unknown. To assess this, we measured the rate of ferricyanide reduction inside liposomes by external ascorbate. Here, we show that MTAs containing ubiquinone (MitoQ series) or plastoquinone (SkQ series) can carry electrons through lipid membranes, with the rate being inversely proportional to the length of the hydrocarbon linker group. Furthermore, this process was stimulated by the hydrophobic anion tetraphenylborate suggesting that permeation of the cationic MTA through the membrane was the rate-limiting step of the process. This conclusion was supported by the observation that the rate of MTA-induced electron transfer was insensitive to nigericin, in contrast to electron transfer mediated by neutral quinone derivatives. These findings indicate that MTAs can be utilized to transfer electrons across lipid membranes and this may be applicable to the study of the electron-transport chain in mitochondria and other natural membranes exhibiting redox processes.

Topics: Cell Membrane; Electron Transport; Ferricyanides; Lipid Bilayers; Phospholipids; Plastoquinone; Ubiquinone

Electron transfers within and between protein complexes are core processes of the electron transport chains occurring in thylakoid (chloroplast), mitochondrial, and bacterial membranes. These electron transfers involve a number of cofactors. Here we describe the derivation of molecular mechanics parameters for the cofactors associated with the function of the photosystem II core complex: plastoquinone, plastoquinol, heme b, chlorophyll A, pheophytin, and β-carotene. Parameters were also obtained for ubiquinol and ubiquinone, related cofactors involved in the respiratory chain. Parameters were derived at both atomistic and coarse grain (CG) resolutions, compatible with the building blocks of the GROMOS united-atom and Martini CG force fields, respectively. Structural and thermodynamic properties of the cofactors were compared to experimental values when available. The topologies were further tested in molecular dynamics simulations of the cofactors in their physiological environment, e.g., either in a lipid membrane environment or in complex with the heme binding protein bacterioferritin.

Topics: beta Carotene; Chlorophyll; Chlorophyll A; Heme; Lipid Bilayers; Molecular Dynamics Simulation; Molecular Structure; Octanols; Pheophytins; Photosystem II Protein Complex; Plastoquinone; Protein Conformation; Thermodynamics; Ubiquinone; Water

In this paper we present theoretical calculations on model biomimetic systems for quinol oxidation. In these model systems, an excited-state [Ru(bpy)(2)(pbim)](+) complex (bpy = 2,2'-dipyridyl, pbim = 2-(2-pyridyl)benzimidazolate) oxidizes a ubiquinol or plastoquinol analogue in acetonitrile. The charge transfer reaction occurs via a proton-coupled electron transfer (PCET) mechanism, in which an electron is transferred from the quinol to the Ru and a proton is transferred from the quinol to the pbim(-) ligand. The experimentally measured average kinetic isotope effects (KIEs) at 296 K are 1.87 and 3.45 for the ubiquinol and plastoquinol analogues, respectively, and the KIE decreases with temperature for plastoquinol but increases with temperature for ubiquinol. The present calculations provide a possible explanation for the differences in magnitudes and temperature dependences of the KIEs for the two systems and, in particular, an explanation for the unusual inverse temperature dependence of the KIE for the ubiquinol analogue. These calculations are based on a general theoretical formulation for PCET reactions that includes quantum mechanical effects of the electrons and transferring proton, as well as the solvent reorganization and proton donor-acceptor motion. The physical properties of the system that enable the inverse temperature dependence of the KIE are a stiff hydrogen bond, which corresponds to a high-frequency proton donor-acceptor motion, and small inner-sphere and solvent reorganization energies. The inverse temperature dependence of the KIE may be observed if the 0/0 pair of reactant/product vibronic states is in the inverted Marcus region, while the 0/1 pair of reactant/product vibronic states is in the normal Marcus region and is the dominant contributor to the overall rate. In this case, the free energy barrier for the dominant transition is lower for deuterium than for hydrogen because of the smaller splittings between the vibronic energy levels for deuterium, and the KIE increases with increasing temperature. The temperature dependence of the KIE is found to be very sensitive to the interplay among the driving force, the reorganization energy, and the vibronic coupling in this regime.

Topics: 2,2'-Dipyridyl; Benzimidazoles; Biomimetic Materials; Hydrogen Bonding; Hydroquinones; Kinetics; Models, Chemical; Organometallic Compounds; Oxidation-Reduction; Plastoquinone; Ruthenium; Temperature; Thermodynamics; Ubiquinone

It was found that plastoquinol-9, ubiquinol-10 and alpha-tocopherol quinol show intrinsic fluorescence in organic solvents and in liposomes. Their fluorescence spectra in solution showed the presence of one emission band with maximum intensity in the range 319.0-327.0 nm for plastoquinol and 321.5-326.5 nm for alpha-tocopherol quinol, which is the longest wavelength shifted in polar solvents. The emission band at about 371 nm for ubiquinol was not sensitive to solvent polarity. For all three prenylquinones the fluorescence quantum efficiency changed significantly in solvents of different polarities, being the highest in ethanol and the lowest in hexane in the case of plastoquinol and alpha-tocopherol quinol, whereas ubiquinol fluorescence showed the opposite effect. These spectral parameters were applied to determination of prenylquinol localization in liposome membranes.

Topics: alpha-Tocopherol; Liposomes; Plastoquinone; Solutions; Spectrometry, Fluorescence; Ubiquinone; Vitamin E