Membrane redox-active

Medina, M. A., Castillo-Olivares, A., and Schwigerer, L., 1992, Plasma membrane redox activity correlates with N-myc expression in neuroblastoma cells, FEBS Lett. 311 99-101. 

Rubinstein, B., and Luster, D. G., 1993, Plasma membrane redox activity Components and role in plant processes, Anna. Rev. Plant Physiol. Plant Mol. Biol. 44 131-155. 

Figure 18.4 Structures of heme/Cu oxidases at different levels of detail, (a) Position of the redox-active cofactors relative to the membrane of CcO (left, only two obligatory subunits are shown) and quinol oxidase (right), (b) Electron transfer paths in mammalian CcO. Note that the imidazoles that ligate six-coordinate heme a and the five-coordinate heme are linked by a single amino acid, which can serve as a wire for electron transfer from ferroheme a to ferriheme as. (c) The O2 reduction site of mammalian CcO the numbering of the residues corresponds to that in the crystal structure of bovine heart CcO. The subscript 3 in heme as and heme 03 signifies the heme that binds O2. The structures were generated using coordinates deposited in the Protein Data Bank, lari [Ostermeier et al., 1997] Ifft [Abramson et al., 2000] (a) and locc [Tsukihara et al., 1996] (b, c).

Cyt c is one of most important and extensively studied electron-transfer proteins, partly because of its high solubility in water compared with other redox-active proteins. In vivo, cyt c transfers an electron from complex III to complex IV, membrane-bound components of the mitochondrial electron-transfer chain. The electrochemical interrogation of cyt c has, however, been hindered because the redox-active heme center is... 

The yeast-mediated enzymatic biodegradation of azo dyes can be accomplished either by reductive reactions or by oxidative reactions. In general, reductive reactions led to cleavage of azo dyes into aromatic amines, which are further mineralized by yeasts. Enzymes putatively involved in this process are NADH-dependent reductases [24] and an azoreductase [16], which is dependent on the extracellular activity of a component of the plasma membrane redox system, identified as a ferric reductase [19]. Recently, significant increase in the activities of NADH-dependent reductase and azoreductase was observed in the cells of Trichosporon beigelii obtained at the end of the decolorization process [25]. 

Ubiquinones (coenzymes Q) Q9 and Qi0 are essential cofactors (electron carriers) in the mitochondrial electron transport chain. They play a key role shuttling electrons from NADH and succinate dehydrogenases to the cytochrome b-c1 complex in the inner mitochondrial membrane. Ubiquinones are lipid-soluble compounds containing a redox active quinoid ring and a tail of 50 (Qio) or 45 (Q9) carbon atoms (Figure 29.10). The predominant ubiquinone in humans is Qio while in rodents it is Q9. Ubiquinones are especially abundant in the mitochondrial respiratory chain where their concentration is about 100 times higher than that of other electron carriers. Ubihydroquinone Q10 is also found in LDL where it supposedly exhibits the antioxidant activity (see Chapter 23). 

In photosynthesis, water oxidation is accomplished by photosystem II (PSII), which is a large membrane-bound protein complex (158-161). To the central core proteins D1 and D2 are attached different cofactors, including a redox-active tyro-syl residue, tyrosine Z (Yz) (158-162), which is associated with a tetranuclear manganese complex (163). These components constitute the water oxidizing complex (WOC), the site in which the oxidation of water to molecular oxygen occurs (159, 160, 164). The organization is schematically shown in Fig. 18. 

There is great interest in the mechanisms of cell death since better understanding might lead to therapy that slows the rate of aging and prevents or treats human disease. Two major processes of cell death have been described, apoptosis and neaosis other alternative pathways generally are variations of these (Formigli et al, 2000 Sperandio et al, 2000 Reed, 1999). Some of the intracellular events related to these types of death have been discovered (Reed, 2000). After exposure to noxious stimuli, the balance between antiapoptotic and proapoptotic influences can result in either survival or death. Many of these variable influences and the subsequent downstream concatenated events involve oxidation, which targets cellular components such as DNA, cellular proteins and membrane phospholipids. Our laboratory and others have studied the role of the redox-active cellular constituents nitric oxide ( NO) and membrane phospholipid... 

Coenzyme Q (ubiquinone) is an essential cofactor in the electron transport chain in which it accepts electrons from complex I and II. Coenzyme Q also serves as an important antioxidant in both mitochondria I and lipid membranes. Coenzyme Q is a lipid-soluble compound composed of a redox active quinoid moiety and a hydrophobic tail. The predominant form of coenzyme Q in humans is coenzyme Q10, which contains ten isoprenoid units in the tail, whereas the predominant form in rodents is coenzyme Q9, which has nine isoprenoid units in the tail. Coenzyme Q is soluble and mobile in the hydrophobic core of the phospholipid bilayer of the inner membrane of the mitochondria in which it transfers electrons one at a time to complex III of the electron transport chain. 

The plasma membranes of plant cells possess several redox activities that can be related to both plant nutrition and cell wall formation and lignification (Liithje et al., 1997 Berczi and Mpller, 2000). In this context, it has been shown that in oat roots, HMS humic fractions inhibited NADH oxidation in either the presence or absence of an artificial electron acceptor (ferricyanide), whereas LMS fractions inhibited this oxidase only if the electron donor (NADH) and acceptor (ferricyanide) were added at the same time (Pinton et al., 1995). While the first effect could be related to the activity of surface peroxidases that can be involved in cell wall formation and thickening (Vianello and Macri, 1991), the second seems to be exerted on a different redox system with an unknown function (Nardi et al., 2002). 

As it has been already indicated in Sect. 2, electron transport through the hydrocarbon core of the bilayer (see reactions (8), (14), (26)) is a key step of any transmembrane PET, and usually it controls the rate and efficiency of the PET process as a whole. Therefore, the data concerning the mechanism of this stage of PET and the factors which affect it are of crucial importance for the development of photochemical systems based on PET across the membranes. Unfortunately, for the majority of the systems listed in Table 1 the proposed mechanisms of electron transfer across the membrane seem to be rather tentative because of insufficient information about the localization of the redox-active components and their diffusion mobility inside the membranes. Only for few systems the studies were detailed enough to propose convincing mechanisms and to give a quantitative description of the kinetics of electron transfer across the membrane. 

One may try to overcome these difficulties by embedding the bridging molecules into bilayer membranes. If their redox active terminal groups are able to undergo reactions with the electron donors and acceptors from aqueous phases, an efficient transmembrane PET will be possible. 

Another way of arranging the intramolecular transmembrane electron transfer is to use the so called molecular wires, i.e. molecules with the electron conduction chain of conjugated bonds, redox active polar terminal groups and the length sufficient to span across the membrane. Such molecules can in principle provide for electron transfer from the externally added or photogenerated reductant across the membrane to the oxidant. This mechanism was suggested [41, 94] to explain the action of carotene-containing System 1 and 38 of Table 1. However, as it was shown later, the transmembrane PET in these systems proceeded also without carotene. 

Fe reduction. Sections of roots can then be viewed under the microscope and the stain located. Bell et al. (1988) have evaluated the use of ferricyanide and the use of nitro-BT, [2,2 -di-/>-nitro-phenyl-5,5 -diphenyl]-3,3 -(3,3 -dimethoxy-4,4 -biphenylene)-di-tetrazolium chloride. With ferricyanide, iron-stressed tomato plants were mainly stained on the younger roots hairs located on the laterals or primary root tip. Nitro-BT is thought to compete with Fe(III) at the same transmembrane ferric reduction site (Sijmons and Bienfate, 1983). A purple diformazan precipitate is produced on reduction. Although the roots were stained in a similar way to those incubated with ferricyanide, Bell et al. (1988) point out that further research is required to determine if nitro-BT reduction completes with ferric reduction at the same site in the tomato. The iron-stress redox activity has been shown to be localised on the plasma membrane in tomato roots (Buckout et al., 1989), and electron microscopic examination (see next section) of the roots stained with Prussian blue indicated that the PB had accumulated between the plasma membrane and the cell walls of the root hairs and epidermal cells (Wergin et al., 1988). 

Liu et al. applied the SECM feedback mode to noninvasively probe the redox activity of individual mammalian cells [70,71]. In order to probe the redox activity of a mammalian cell, both oxidized and reduced forms of the redox mediator must be capable of crossing the cell membrane and shuttling the charge between the tip electrode and the intracellular redox centers (Fig. 23a). Only hydrophobic redox mediators (e.g., menadione and 1,2-naphthoquinone) could be used in SECM experiments with mammalian cells [71]. The redox reactions at the tip and inside the cell can be presented as follows ... 

Dependent upon the nature of the immobilized cells and the lipophilicity of the mediator molecule, the reduced mediator may be formed at redox active sites on the outside of the plasma membrane or at sites within the... 

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