Oxygen catalytic mechanisms

The chemistry of the stratospheric ozone will be sketched with a very broad brush in order to illustrate some of the characteristics of catalytic reactions. A model for the formation of ozone in the atmosphere was proposed by Chapman and may be represented by the following "oxygen only" mechanism (other aspects of... 

This simple oxygen-only mechanism consistently overestimates the O3 concentration in the stratosphere as compared to measured values. This implies that there must be a mechanism for ozone destruction that the Chapman model does not account for. A series of catalytic ozone-destroying reactions causes the discrepancy. Shown below is an ozone-destroying mechanism with NO/NO2 serving as a catalyst ... 

A typical result for DPV In Fig. 4a shows the presence of two redox couples with peak potentials of 0.25 V and 0.19 V ( lOmV). Similar results have also been obtained with SWV. The relative Intensities of the two peaks vary from sample to sample but are always present with activated electrodes. The similarities between the potentials found for the surface species and for the oxidation of ascorbic acid suggest that an ec catalytic mechanism may be operative. The surface coverage of the o-qulnone Is estimated to be the order of 10 mol cm . It Is currently not possible to control the surface concentration of the o-qulnone-llke species or the oxygen content of the GCE surface. 

Luo, J., Zhang, Q., Garcia-Martinez, J. and Suib, S.L. (2008) Adsorptive and acidic properties, reversible lattice oxygen evolution, and catalytic mechanism of cryptomelane-type manganese oxides as oxidation catalysts. Journal of the American Chemical Society, 130, 3198-3207. 

The organometallic complexes with d-metals are considered as promising electrocatalysts for oxygen electroreduction in air-metal electrochemical cells. Obviously, the first idea was to employ the catalytic mechanism of the oxygen reduction with porphyrin-like metal complexes [1] found in living beings (Figure 1). 

Fig. 20. Frame-by-frame series of stop-action pictures of the catalytic mechanism of RNase A at atomic resolution. Only the essential active site residues and the substrate (filled bonds) are shown. Frame 1, l e native enzyme. The sulfate ion which binds to the active site is shown. Frame 2, The Michaelis E-S complex with the dinucleotide CpA. The 2 oxygen which is deprotonated by His-12 is blackened. Frame 3, The transition state for...

In this conformation, the N-acetyl carbonyl oxygen is foimd only 3.0 A from the anomeric carbon, in a position favorable for nucleophiUc attack on Cl and formation of an oxazolinum ion, which is the first step in the substrate-assisted catalytic mechanism of family 18 enzymes. 

The data for the p-phenylenediamine-silver ion reaction are not accounted for by Bagdasar yan s treatment. On the basis of an adsorption mechanism, the data would suggest that the important phase for the catalyzed reaction is adsorption of the p-phenylenediamine by the silver catalyst. The extent of the adsorption would depend upon the surface conditions of the catalyst, which apparently depend on changes in the protective colloid or in the salt concentration. A catalytic mechanism involving activation of the p-phenylenediamine by the catalyst would be consistent with the observation of Weissberger and Thomas that colloidal silver markedly catalyzes the oxygen oxidation of p-phenylenediamine. 

A systematic study on enzymatic catalysis has revealed that isolated enzymes, from baker s yeast or old yellow enzyme (OYE) termed nitroalkene reductase, can efficiently catalyze the NADPH-linked reduction of nitroalkenes. Eor the OYE-catalyzed reduction of nitrocyclohexene, a catalytic mechanism was proposed in which the nitrocyclohexene is activated by nitro-oxygen hydrogen bonds to the enzymes His-191 and Asn-194 [167, 168]. Inspired by this study Schreiner et al. 

It is supposed that the catalytic mechanism proceeds through a free-radical intermediate which reacts directly with oxygen or an organic iron intermediate [63]. The three-dimensional protein structure of the native form of LOX isoenzyme L-1 from soybean has already been described [64, 65]. 

A catalytic mechanism (Figure 14) was proposed on the basis of kinetic, spectroscopic and crystallographic data . The substrate peptide binds to Zn2 with its N-terminal amino group and to Znj with the carbonyl oxygen of the scissile peptide bond. Additionally, the N-terminus interacts with Aspl79. Upon substrate binding, the bridging water... 

Silver ion also catalyzes nucleophilic reactions of thiol esters, including reactions of acetylhomocysteine thiolactone (12) and diethylethylphosphonothiolate (52). In the first reaction, an insoluble complex of silver ion and the substrate was first produced at pH 7.5, which then reacted with the nucleophile, in this case an amino group of a protein. In the second reaction silver ion complexes of the substrate were also postulated, on the basis that silver ion complexes with sulfur are much more stable than those with oxygen (I). The complexes postulated were 1 1 and 2 1 silver ion-substrate complexes. These complexes were suggested to react with the nucleophiles, water and fluoride ion, giving as products phos-phonic acid and phosphonyl fluoride, respectively, and silver mercaptide. It is evident that the last reaction at least must involve only the direct interaction of a silver ion with the sulfur atom of the thiol ester without chelate formation. Therefore it appears the metal ion-catalyzed reactions of thiol esters are unique, in that they involve complex formation, but not chelate formation in their catalytic mechanism. 

A determination of the pH dependence of the lanthanum hydroxide gel-promoted hydrolysis of /3-glyceryl phosphate revealed that the two maxima exist in the pH-rate profile, one at pH 8.6 which presumably involves the species La (OH)+2 and another (smaller) maximum at pH 10.4 which involves the species La (OH) 2+ (4). Presumably the same kind of catalytic mechanism is operative in both cases. These reactions may serve as models for the metal ion-promoted alkaline phosphatases which have been shown to proceed with P—O cleavage (and with no oxygen exchange). 

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