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Covalent bonds Breaking

Complex ions used for electroplating are anions. The cathode tends to repel them, and their transport is entirely by diffusion. Conversely, the field near the cathode assists cation transport. Complex cyanides deserve some elaboration in view of their commercial importance. It is improbable that those used are covalent co-ordination compounds, and the covalent bond breaks too slowly to accommodate the speed of electrode reactions. The electronic structure of the cyanide ion is ... [Pg.345]

Fig. 4 Halogen-bonded adducts are pre-reactive complexes, which, under convenient conditions, can lead to covalent bonds breaking and forming. Perfluoroalkylation occurs when the complexes between iodoperfluoroalkanes and anilines are heated or irradiated in certain solvents... Fig. 4 Halogen-bonded adducts are pre-reactive complexes, which, under convenient conditions, can lead to covalent bonds breaking and forming. Perfluoroalkylation occurs when the complexes between iodoperfluoroalkanes and anilines are heated or irradiated in certain solvents...
Ionic reactions are those in which covalent bonds break heterolytically, and in which ions are involved as reactants, intermediates, or products. [Pg.364]

Chlorine molecules (Cl2) absorb the u.v. light and the (Cl—Cl) covalent bonds break to form two chlorine atoms ... [Pg.88]

When a covalent bond breaks to produce radicals, i.e. one electron of the bond pair goes to each atom, homolytic fission has occurred. These highly reactive chlorine radicals attack the methane molecules. [Pg.88]

Although hydrogen bonding is a strong form of intermolecular attraction, it is much weaker than a normal C—H, N—H, or O—H covalent bond. Breaking a hydrogen bond requires about 20 kJ/mol (5 kcal/mol), compared with about 400 kJ/mol (about 100 kcal/mol) required to break a C — H, N—H, or O — H bond. [Pg.68]

The most probable mechanism for the rate determining step involves a transition state, such as 3, in which the proton transfer either precedes or is concerted with covalent bond breaking. The mechanisms of orthoester hydrolysis have been summarized and discussed by DeWolfe and Jensen (1963), Wenthe and Cordes (1964), Bunton and DeWolfe (1966), Cordes (1967), DeWolfe (1969), and Jencks (1969). [Pg.310]

This book starts with a discussion of how covalent bonds break and form, and how these bond-breaking and bond-forming processes provide the basis of reaction mechanisms. The principles governing how to make sensible suggestions about possible mechanisms are set out, and the distinction is made between elementary reactions, which involve just one step, and stepwise reactions which have more than one step and involve the production of intermediates that react further. [Pg.206]

For simple covalent bond breaking reactions, a bound state in the R-BO scheme correlates to a diradical asymptotic state. This latter state represents in the laboratory world a collision pair. In a-space we can define an intermolecular distance. For all values of such distance, the system cannot change its electronic state in an adiabatic process. The asymptotic state must be orthogonal to the bound state. It is therefore necessary that the electronic wave function of the collision pair show one node more than the bounded system. The energy expectation values as a function of the intermolecular distance for the two states would cross above the dissociation energy limit. The corresponding FC factor can hence be different from zero. Experimentally, it is well known that most of the bond-forming processes may have a small barrier (about 1 Kcal/mol) [22]. [Pg.119]

In a symmetrical cleavage, when a covalent bond breaks, each of the constituent atoms retains one electron (represented by a dot or circle) from the bond that is cleaved... [Pg.145]

Severai detaiied reviews on the stabiiity of proteins and protein pharmaceuticais written for pharmaceutical scientisls are available (43,45,46,47,48,49,50). A brief overview of these resources foiiows and provides additionai information. The instability of proteins, including protein pharmaceuticals, can be separated into two distinct ciasses. Chemicai instabiiity resuits from bond formation or cleavage yielding a modification of the protein and a new chemical entity. Physical instability involves a change to the secondary or higher-order structure of the protein rather than a covalent bond-breaking modification. [Pg.221]

Although in this region there is contact between an alkyl halide and cyanide anions, because of its very small volume and rather moderate rate constant of the reaction that proceeds via covalent bond breaking, the observed rate of substitution in this region is negligible. [Pg.193]

Is when a covalent bond breaks by splitting the shared pair of bonding electrons between the two products Produces two free radicals, each having an unpaired electron... [Pg.672]

Is when a covalent bond breaks with both the shared electrons going to one of the products Produces two oppositely charged ions... [Pg.672]

Chemists use curved arrows to show how electrons move as covalent bonds break and/or new covalent bonds form. The tail of the arrow is positioned at the point where the electrons are in the reactant, and the head of the arrow points to where these same electrons end up in the product. [Pg.225]


See other pages where Covalent bonds Breaking is mentioned: [Pg.125]    [Pg.125]    [Pg.242]    [Pg.88]    [Pg.72]    [Pg.231]    [Pg.78]    [Pg.78]    [Pg.230]    [Pg.528]    [Pg.268]    [Pg.242]    [Pg.231]    [Pg.24]    [Pg.2291]    [Pg.3355]    [Pg.2329]    [Pg.126]    [Pg.494]    [Pg.223]    [Pg.133]    [Pg.267]    [Pg.984]    [Pg.244]    [Pg.102]    [Pg.143]    [Pg.2284]    [Pg.3021]    [Pg.526]    [Pg.281]   
See also in sourсe #XX -- [ Pg.48 , Pg.79 , Pg.80 , Pg.81 , Pg.82 , Pg.83 , Pg.84 , Pg.85 , Pg.86 , Pg.87 , Pg.88 , Pg.89 , Pg.90 , Pg.91 , Pg.92 , Pg.93 , Pg.94 , Pg.339 ]




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