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Transfer across membranes structure

Facilitated diffusion is very similar to passive diffusion with the difference that transfer across membranes is assisted by the participation of carrier proteins embedded in the membrane bilayer. Again, the direction of passage will be from the side of the membrane with high concentration of a chemical to the side with low concentration this also occurs without energy expenditure by the cell. Such a process is somewhat specific in the sense that it applies to molecules that are able to bind to a carrier protein. Absorption of nutrients such as glucose and amino acids across the epithelial membrane of the gastrointestinal tract occurs by facilitated diffusion. Since a finite number of carriers are available for transport, the process is saturable at high concentrations of the transported molecules and competition for transport may occur between molecules of similar structure. [Pg.2]

Active transport requires a specialized carrier molecule, a protein, and the expenditure of cellular energy transfer across membranes can therefore occur against a concentration gradient. The carrier system is selective for certain structural features of chemicals, namely their ionized state, whether anionic, cationic, or neutral. Recent advances in the understanding of active transport have led to the characterization of several families of carriers. Such carrier systems are saturable. In addition, molecules with similar structural features may compete for transport by a given carrier. [Pg.2]

There are as yet no conclusions nor even a consensus hypothesis as to which types of chlorine substitution patterns govern ease of metabolism by enzymes. Some researchers favor the hypothesis that chlorine substitution at the 4,4 or combinations at the 3,5 3 5 positions of the biphenyl molecule block ease of enzymatic epoxidation of easily accessible vicinal carbons (14, 35). Other researchers suggest that 2,2 or 6,6 substitutions or some combination reduce coplanarlty of the biphenyl rings thereby causing a steric hlnderance to enzymatic activity or transfer across membranes (14, 36). Our data on Individual chloroblphenyla In biota does not yet encompass a wide enough range of chloroblphenyl structures to test these hypotheses which must be tested rigorously with Isotopically labeled chloroblphenyla In carefully controlled experiments In any event. [Pg.194]

The structurally similar L and M subunits are related by a pseudo-twofold symmetry axis through the core, between the helices of the four-helix bundle motif. The photosynthetic pigments are bound to these subunits, most of them to the transmembrane helices, and they are also related by the same twofold symmetry axis (Figure 12.15). The pigments are arranged so that they form two possible pathways for electron transfer across the membrane, one on each side of the symmetry axis. [Pg.237]

The surface characteristics of these species are determined by the particulates and stress transfer across the membrane will tend to be low, reducing internal circulation within the drop. The structure of the interface surrounding the drop plays a significant role in determining the characteristics of the droplet behaviour. We can begin our consideration of emulsion systems by looking at the role of this layer in determining linear viscoelastic properties. This was undertaken by... [Pg.279]

The publication of Pedersen s work attracted instant and increasing attention from a variety of scientists worldwide. During the ensuing decade, research in an increasing number of laboratories led to the synthesis and characterization of many novel macrocychc chemical structures, and to the application of macrocycles in a wide variety of fields. This effort cut across many areas including organic and inorganic synthesis, biochemistry, ion transport in membranes, phase transfer catalysis, and structure analysis. [Pg.1]

The definitions of effective diffusivity tensors are key parameters in the solution of the transport equations above. For an isotropic medium, the effective diffusivity is insensitive to the detailed geometric structure, and the volume fraction of the phases A and B influences the effective diffusivity. When the resistance to mass transfer across the cell membrane is negligible, the isotropic effective diffusivity, Ds e = Dg eI may be obtained from Maxwell s equation... [Pg.566]

As imphed by equation (3), and by the location of the O2 reduction site in the structure, proton transfer across the cytochrome oxidase protein is required for function, which necessitates proton-conducting pathways for three specific purposes, that is, to transfer the four substrate protons from the A-side of the membrane into the site of O2 reduction, for uptake of the four pumped protons (per O2 reduced) that are translocated across the membrane coupled to the redox reaction, and for release of these protons to the opposite side of the membrane (exit pathway). Site-directed mutagenesis data indicated the presence of two proton transfer pathways from the A-side of the membrane toward the binuclear heme... [Pg.1057]

These examples should serve to underscore the difficulty in predicting the effects that interfacial potentials, membrane structure and microphase organization will have on electron-transfer reactions across the membrane interface and within the bilayer itself. The principles involved are common to micelles and vesicles, but the more anisotropic and highly ordered vesicles provide a more complex reaction environment for solubilized or adsorbed reactants. [Pg.2980]

Fig. 3 Left Schematic representation of a DNA-loaded triblock-based polymersome. The virus, a X phage, binds a LamB protein and the DNA is transferred across the block copolymer membrane. Right An electron micrograph of negatively stained complexes formed between X phage and vesicles bearing LamB proteins at 37° C. The X phage (large structure on the top left comer) is attached to one vesicle via its tail. Ref. [27]. Copyright (2002) National Academy of Sciences, U.S.A... Fig. 3 Left Schematic representation of a DNA-loaded triblock-based polymersome. The virus, a X phage, binds a LamB protein and the DNA is transferred across the block copolymer membrane. Right An electron micrograph of negatively stained complexes formed between X phage and vesicles bearing LamB proteins at 37° C. The X phage (large structure on the top left comer) is attached to one vesicle via its tail. Ref. [27]. Copyright (2002) National Academy of Sciences, U.S.A...
An ion, on the other hand, is of the same general size as parts of the structure to which it migrates. The proton is perhaps a limiting case in that there may be a number of sites to which it can migrate, as the facility with which aqueous systems conduct protons shows [75,76], Nevertheless, a structure, a membrane surface for example, that admits ion transfer across the boundary at particular points can indeed reveal sites that are of the size of the probe. The interpretation of the... [Pg.113]

Because membranes are dynamic structures, the mechanism by which they are synthesized is complex. Currently, little is known about the synthesis of the membrane bilayer except for the following features phospholipid translocation across membranes and the intracellular transfer of phospholipids between membranes. [Pg.404]

Hydrogen transfer is one of the most pervasive and fundamental processes that occur in biological systems. Examples include the prevalent role of acid-base catalysis in enzyme and ribozyme function, the activation of C-H bonds leading to structural transformations among a myriad of carbon-based metabolites, and the transfer of protons across membrane bilayers to generate gradients capable of driving substrate transport and ATP biosynthesis. [Pg.1241]

By means of suitable membrane-active additives, we have attempted to modify the structure of isolated thylakoids and thereby increase membrane permeability. Changes in resistance of the membranes to freezing were then determined. Figure 11 shows the effect of sodium caprylate on the permeability of thylakoids to protons. In the absence of the compound, illumination causes proton transfer across the thylakoids and acidification of the intrathylakoid space. A fluorescent weak amine was used to monitor formation of the proton gradient (86). When the light was turned off, protons moved slowly back across the thylakoid membrane. Transport followed first-order kinetics. In the presence of caprylate... [Pg.185]

Structure and Mechanism. Cytochrome-c oxidase catalyzes the four-electron reduction of molecular oxygen to water and couples these redox processes to proton transfer across the mitochondrial membrane.As depicted in Fig. 24, the enzyme is structurally complex and contains four metal centers which are redox active, two copper ions and two heme a groups. One copper ion, Cug, and one of the heme a groups, cytochrome <13, (cyt a ), form a binuclear center which binds dioxygen. Electrons are ... [Pg.491]

The coupling of these two reactions requires that charge is capable of being transferred across the membrane, most probably through the membrane-bound protein structures. The experimental and theoretical studies of charge transport in protein structures has been extensively reviewed elsewhere.The potential difference AV across the membrane would then have the value... [Pg.216]

One investigative study that has raised considerable queries is the report of direct electrical communication between the active site of the enzyme and the conducting polymer when the enzyme is immobilized in polypyrrole microtubules. These microtubules were produced by electropolymerization of the pyrrole monomer inside the pores of a microporous filtration membrane. This configuration is reported to favor direct electron transfer across the polymer structure as well as direct reoxidation of the enzyme at lower potentials than typically used, hence promoting increased selectivity of the resulting amperometric biosensor [178]. Another report investigating the same system claims that it is the underlying platinum metal rather than polypyrrole tubules that is responsible for the observed direct enzyme reoxidation [179]. [Pg.1515]


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