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Nitrogen oxidation electron transfer

The generation of nitrogen containing radicals is connected with oxidative electron-transfer reactions initiated by dimers of NO in phenol units and nonphenolic structures. The subsequent radical conversions include processes of degradation and modification (i.e., nitrosation and nitration) of lignin. [Pg.471]

Because the breadth of chemical behavior can be bewildering in its complexity, chemists search for general ways to organize chemical reactivity patterns. Two familiar patterns are Br< )nsted acid-base (proton transfer) and oxidation-reduction (electron transfer) reactions. A related pattern of reactivity can be viewed as the donation of a pair of electrons to form a new bond. One example is the reaction between gaseous ammonia and trimethyl boron, in which the ammonia molecule uses its nonbonding pair of electrons to form a bond between nitrogen and boron ... [Pg.1499]

Fig. 6.9 The catalysts for denitrification. Nitrate is reduced by a molybdenum enzyme while nitrite and oxides of nitrogen are reduced today mainly by copper enzymes. However, there are alternatives, probably earlier iron enzymes. The electron transfer bct complex is common to that in oxidative phosphorylation and similar to the bf complex of photosynthesis, while cytochrome c2 is to be compared with cytochrome c of oxidative phosphorylation. These four processes are linked in energy capture via proton (H+) gradients see Figure 6.8(a) and (b) and the lower parts of Fig. 6.9 which show separately the active site of the all iron NO-reductase, and the active site of cytochrome oxidase (02 reductase). Fig. 6.9 The catalysts for denitrification. Nitrate is reduced by a molybdenum enzyme while nitrite and oxides of nitrogen are reduced today mainly by copper enzymes. However, there are alternatives, probably earlier iron enzymes. The electron transfer bct complex is common to that in oxidative phosphorylation and similar to the bf complex of photosynthesis, while cytochrome c2 is to be compared with cytochrome c of oxidative phosphorylation. These four processes are linked in energy capture via proton (H+) gradients see Figure 6.8(a) and (b) and the lower parts of Fig. 6.9 which show separately the active site of the all iron NO-reductase, and the active site of cytochrome oxidase (02 reductase).
Electron-transfer activation. The observation of intense coloration upon mixing the solutions of hydroquinone ether MA and nitrogen dioxide at low temperature derives from the transient formation of MA+ cation radical, as confirmed by the spectral comparison with the authentic sample. The oxidation of MA to the corresponding cation radical is effected by the nitrosonium oxidant, which is spontaneously generated during the arene-induced disproportionation of nitrogen dioxide,239 i.e.,... [Pg.286]

Peroxynitrite reacts with heme proteins such as prostacycline synthase (PGI2), microperoxidase, and the heme thiolate protein P450 to form a ferryl nitrogen dioxide complex as an intermediate [120]. Peroxynitrite also reacts with acetaldehyde with the rate constant of 680 1 mol 1 s" 1 forming a hypothetical adduct, which is decomposed into acetate, formate, and methyl radicals [121]. The oxidation of NADH and NADPH by peroxynitrite most certainly occurs by free radical mechanism [122,123], Kirsch and de Groot [122] concluded that peroxynitrite oxidized NADH by a one-electron transfer mechanism to form NAD and superoxide ... [Pg.704]

In the mechanism study of /V-benzyl-/V -alkyl hydroxylamines, regarding oxidation with HgO and p-benzoquinone, it has been proposed on the basis of intra- and intermolecular kinetic isotope effects that, initially, there takes place a one-electron transfer from a nitrogen atom to the oxidant, with a subsequent proton abstraction (106—108). [Pg.143]

Iron, Fe2+ (d6) Iron, Fe2+ (d6) 4, tetrahedral 6, octahedral N-Thiolate O-Carboxylate, alkoxide, oxide, phenolate Electron transfer, nitrogen fixation in nitrogenases, electron transfer in oxidases... [Pg.4]

It is also assumed (Hoffmann 1990) that the adsorbed sulfite is oxidized by the valence band holes, h+b, that are formed through absorption of light with photon energies exceeding the band-gap energy (ca. 2.2 eV) of an iron(III)(hydr)oxide, e.g., hematite (a-Fe203). This interfacial electron transfer reaction results in formation of the SO radical anion which reacts with another radical to form S20 , one of the end product, if the reaction is carried out under nitrogen. [Pg.355]

Chemoselective anodic methoxylation at a distinct carbon atom in the a-position to an amino group in a polypeptide was achieved by prior introduction of a silyl group as an electroauxiliary at this carbon atom [156]. Amide oxidation in A-acetylpyrrolidines substituted with electron-rich phenyl rings led to either methoxylation a to the nitrogen atom or in the benzylic position. Mechanistic studies indicate that both the amide and the phenyl oxidation compete, but intramolecular electron transfer leads to... [Pg.418]


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See also in sourсe #XX -- [ Pg.193 ]




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Electron Oxidants

Electron transfer, oxides

Electronic oxides

Electrons oxidation

Nitrogen electrons

Nitrogen transfer

Oxidation transfer

Oxidative electron transfer

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