Stereospecificity heterogeneously catalyzed

Fig. 3.22. Stereoselectivity and stereospecificity of a pair of heterogeneously catalyzed hydrogenations.

The classical heterogeneously catalyzed propene polymerization as discovered hy Natta is a stereospecific reaction forming a polymer with isotactic microstructure. During the development of single-site polymerization catalysts it was found that C2-symmetric chiral metallocene complexes own the same stereospecificity. An analysis of the polymer microstructure hy means of NMR spectroscopy revealed that misinsertions are mostly corrected in the next insertion step, which suggests stereocontrol (Figure 6) hy the coordination site, as opposed to an inversion of stereospecificity hy control from the previous insertion steps (chain-end control). In addition, it was found that Cs-symmetric metallocene catalysts lead to syndio-tactic polymer since the Cosee-Arlmann chain flip mechanism induces an inversion of the stereospecificity at every insertion step. This type of polymer was inaccessible by classical heterogeneous systems. 

The stereospecific polymerization of alkenes is catalyzed by coordination compounds such as Ziegler-Natta catalysts, which are heterogeneous TiCl —AI alkyl complexes. Cobalt carbonyl is a catalyst for the polymerization of monoepoxides several rhodium and iridium coordination compounds... 

Of the many reagents, both heterogeneous and homogeneous, that can facilitate chemical reactions, the cycloamyloses stand out. Reactions can be catalyzed with many species such as hydronium ions, hydroxide ions, general acids, general bases, nucleophiles, and electrophiles. More effective catalysis can sometimes be achieved by combinations of catalytic species as in multiple catalysis, intramolecular catalysis, and catalysis by com-plexation. Only the latter catalysis can show the real attributes of an efficient catalytic system, namely speed and selectivity. In analogy to molecular sieves, selectivity can be attained by stereospecific complexation and speed can be likewise attained if the stereochemistry within the complex is correct. The cycloamyloses, of any simple chemical compound, come the closest to these goals. 

The zeolite is rigid and ordered, and lacks conformational adaptability, in contrast to an enzyme, which can coil, uncoil, and twist around. Yet the zeolite can incorporate transition metal functions—these are of prime importance in enzyme catalysis—and it can effect redox reactions reactions over zeolites can be inhibited by competitive adsorption of reactants, products, solvents, or poisons—a phenomenon observed in biological and some other inorganic heterogeneous catalytic systems Rideal kinetics have been identified in some zeolite-catalyzed alkylations, a pattern which has its parallels in the enzyme field a few cases of stereospecificity (such as orfho-alkylation effects, unusual olefin isomer ratios), where a transition state not otherwise attainable intervenes, may exist. What better group of catalysts than zeolites might there have been to activate the evolutionary process in the dark, fermenting Pre-Cambrian seas some 1,000,000,000 years ago ... 

At the present time, the most likely concept of the mechanism of a heterogeneous polymerization catalyzed by a Ziegler-Natta catalyst involves a complex in which the organometallic component and the transition metal component—i.e., the A1 and Ti atoms—are joined by electron-deficient bonds. Natta, Corradini, and Bassi (13) have reported such a structure for the active catalyst prepared from bis (cyclopentadienyl) titanium dichloride and aluminum triethyl. Natta and Pasquon (14), Patat and Sinn (18), and Furukawa and Tsuruta (2) have proposed mechanisms for the stereospecific polymerization of a-olefins in terms of such electron-deficient complexes. 

Enzymes are highly stereospecific in binding chiral substrates and in catalyzing reactions. This stereospecificity arises because enzymes are made of L-amino acids and form asymmetric active sites. Similar to homogeneous and heterogeneous catalysis, chemical reactions proceed on active sites of enzymes, which represent a small part of the total protein. 

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