Efficiency, catalytic

As catalysts, enzymes are highly efficient. The catalytic efficiency, in its simplest form, is that an enzyme that operates with maximal efficiency wiU catalyze the reaction of every 

TABLE 11.2 Comparison of catalytic power of various catalysts 

Approximation and orientation This is the entropic contribution (Page, 1977). Enzymatic reactions take place in the confines of the enzyme-substrate complex. The catalytic groups are part of the same complex as the substrate. This proximity/propinquity and appropriate positioning of substrate molecules with respect to the catalytic groups in the active site via stereopopulation control or orbital steering may contribute to a rate enhaucement with a factor of 10 to 10.  

Substrate anchoring The substrate anchoring (Reuben, 1971) may be visualized as having the effect of increasing the probability of forming the activated complex. 

Strain and distortion The substrate molecule, by forming the enzyme-substrate complex, is forced toward the geometry of the transition state since the enzyme may bind the transition-state-like structure favorably (Secemski and Lienhard, 

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In this section the catalytic efficiency of Co(DS)2, Ni(DS)2, Cu(DS)2 andZn(DS)2 micelles as well as the effect of CTAB and C12E7 on the copper-ion catalysed Diels-Alder reaction between 5.1 and 5.2 is described... 

Interestingly, at very low concentrations of micellised Qi(DS)2, the rate of the reaction of 5.1a with 5.2 was observed to be zero-order in 5.1 a and only depending on the concentration of Cu(DS)2 and 5.2. This is akin to the turn-over and saturation kinetics exhibited by enzymes. The acceleration relative to the reaction in organic media in the absence of catalyst, also approaches enzyme-like magnitudes compared to the process in acetonitrile (Chapter 2), Cu(DS)2 micelles accelerate the Diels-Alder reaction between 5.1a and 5.2 by a factor of 1.8710 . This extremely high catalytic efficiency shows how a combination of a beneficial aqueous solvent effect, Lewis-acid catalysis and micellar catalysis can lead to tremendous accelerations. 

Km for an enzymatic reaction are of significant interest in the study of cellular chemistry. From equation 13.19 we see that Vmax provides a means for determining the rate constant 2- For enzymes that follow the mechanism shown in reaction 13.15, 2 is equivalent to the enzyme s turnover number, kcat- The turnover number is the maximum number of substrate molecules converted to product by a single active site on the enzyme, per unit time. Thus, the turnover number provides a direct indication of the catalytic efficiency of an enzyme s active site. The Michaelis constant, Km, is significant because it provides an estimate of the substrate s intracellular concentration. 

Elucidating Mechanisms for the Inhibition of Enzyme Catalysis An inhibitor interacts with an enzyme in a manner that decreases the enzyme s catalytic efficiency. Examples of inhibitors include some drugs and poisons. Irreversible inhibitors covalently bind to the enzyme s active site, producing a permanent loss in catalytic efficiency even when the inhibitor s concentration is decreased. Reversible inhibitors form noncovalent complexes with the enzyme, thereby causing a temporary de-... 

Engineering Substrate Specificity. Although the serine proteases use a common catalytic mechanism, the enzymes have a wide variety of substrate specificities. For example, the natural variant subtiHsins of B. amyloliquefaciens (subtiHsin BPN J and B. licheniformis (subtiHsin Carlsberg) possess very similar stmctures and sequences where 86 of 275 amino acids are identical, but have different catalytic efficiencies, toward tetraamino acid -nitroanilide substrates (67). 

The characteristics of enzymes are their catalytic efficiency and their specificity. Enzymes increase the reaction velocities by factors of at least one million compared to the uncatalyzed reaction. Enzymes are highly specific, and consequendy a vast number exist. An enzyme usually catalyzes only one reaction involving only certain substrates. For instance, most enzymes acting on carbohydrates are so specific that even the slightest change in the stereochemical configuration is sufficient to make the enzyme incompatible and unable to effect hydrolysis. 

Catalytic Unit. The catalytic unit consists of an activated coating layer spread uniformly on a monolithic substrate. The catalyst predominantly used in the United States and Canada is known as the three-way conversion (TWC) catalyst, because it destroys aU three types of regulated poUutants HC, CO, and NO. Between 1975 and the early 1980s, an oxidation catalyst was used. Its use declined with the development of the TWC catalyst. The TWC catalytic efficiency is shown in Figure 5. At temperatures of >300° C a TWC destroys HC, CO, and NO effectively when the air/fuel mixture is close to... 

A final important area is the calculation of free energies with quantum mechanical models [72] or hybrid quanmm mechanics/molecular mechanics models (QM/MM) [9]. Such models are being used to simulate enzymatic reactions and calculate activation free energies, providing unique insights into the catalytic efficiency of enzymes. They are reviewed elsewhere in this volume (see Chapter 11). 

That is, k t/K,n is an apparent second-order rate constant ior the reaction of E and S to form product. Because A , is inversely proportional to the affinity of the enzyme for its substrate and is directly proportional to the kinetic efficiency of the enzyme, A , provides an index of the catalytic efficiency of an enzyme operating at substrate concentrations substantially below saturation amounts. 

The nickel and cohalt aqua complexes were even more effective, both for catalytic activity and enantioselectivity, than the corresponding anhydrous complexes (Scheme 7.5). Addition of three equivalents of water to the anhydrous nickel complex recovered the catalytic efficiency. DBFOX/Ph complexes derived from manga-nese(II), iron(II), copper(II), and zinc(II) perchlorates, both anhydrous and vef. 

Cordes et al995 carried out alkaline hydrolyses of p-nitrophenylhexanoate 55 (PNPH) in the presence of poly-4-vinylpyridine partially quaternized with dodecyl-bromide and ethylbromide (QPVP). They also found that the polyelectrolytes are increasingly effective as catalysts with an increasing ratio of dodecyl to ethyl groups, and the hydrophobic interactions are important in determining the catalytic efficiency. They observed the inhibitory effects of several gegen-anions fluoride ions are the weakest inhibitor, and nitrate is the strongest (F- < Cl < S04 [Pg.159]

The catalytic efficiency increases, under comparable conditions (pH, concentration of catalyst, etc.) in the sequence Cl < Br - S(CH3)2 < SCN < SC(NH2)2 < I . Titration with a calibrated solution of NaN02 (usually 0.05 to 0.10 m) is used for the analytical determination of aromatic amines, dissolved in aqueous H2S04 or HC1. Here nucleophilic catalysis is achieved by adding KBr. This allows a titration to be completed much faster than without that addition. 

The data in Table 3-1 demonstrate, however, that the sequence of catalytic efficiency mentioned above is caused not by higher nitrosation reactivity k2 of the respective nitroso compounds XNO, but by the more favorable position of the equilibrium in Scheme 3-26, i.e., by higher values for A"Xno-... 

Bifunctional catalysis in nucleophilic aromatic substitution was first observed by Bitter and Zollinger34, who studied the reaction of cyanuric chloride with aniline in benzene. This reaction was not accelerated by phenols or y-pyridone but was catalyzed by triethylamine and pyridine and by bifunctional catalysts such as a-pyridone and carboxylic acids. The carboxylic acids did not function as purely electrophilic reagents, since there was no relationship between catalytic efficiency and acid strength, acetic acid being more effective than chloracetic acid, which in turn was a more efficient catalyst than trichloroacetic acid. For catalysis by the carboxylic acids Bitter and Zollinger proposed the transition state depicted by H. 

Certain substances known as competitive inhibitors, symbolized I, may lower the catalytic efficiency of the enzyme (or other catalyst) by binding to it. Consider that the E I complex has a dissociation constant K. ... 

Furthermore, it was found that, although the catalytic efficiency measured in initial current was lower for 13, the latter was more stable. When carbon felt electrodes were coated with this polymer (approx. 1 x 10 mol on a 20x20x4 mm piece) the reduction of dibromostilbene was obtained on a mmol scale with only moderate da rease of mediator electroactivity The production of about 0.15 mmol of stilbene... 

PMc3 to give the complex salts 21 as shown in Scheme 12. Compounds of type 20 and 21 have successfully been tested for their catalytic efficiency. However, it was observed that fBuaPNSiMea failed to show similar adduct formation and this failure was attributed to steric crowding. 

In the enzyme design approach, as discussed in the first part of this chapter, one attempts to utilize the mechanistic understanding of chemical reactions and enzyme structure to create a new catalyst. This approach represents a largely academic research field aiming at fundamental understanding of biocatalysis. Indeed, the invention of functional artificial enzymes can be considered to be the ultimate test for any theory on enzyme mechanisms. Most artificial enzymes, to date, do not fulfill the conditions of catalytic efficiency and price per unit necessary for industrial applications. 

In industrial processes, 1,3-propanediol is used for the production of polyester fibers, polyurethanes and cydic compounds [85]. 1,3-Propanediol can be produced from glucose with the limiting step catalyzed by glycerol dehydratase. A metagenomic survey for glycerol hydratases from the environment resulted in seven positive clones, one of which displayed a level of catalytic efficiency and stability making it ideal for application in the produdion of 1,3-propanediol from glucose. 

As shown in Table IV, the highest catalytic activity of metal halides used as Lewis acid for the alkylation reaction of ferrocene with 2 was observed in methylene chloride solvent. Among Lewis acids such as aluminum chloride, aluminum bromide, and Group 4 transition metal chlorides (TiCl4, ZrCU, HfCU), catalytic efficiency for the alkylation decrea.ses in the following order hafnium chloride > zirconium chloride > aluminum chloride > aluminum bromide. Titanium chloride... 

From the results of the urease activity test summarized in Figure 15, it is clear that the deposition procedure preserved to a certain extent the enzyme catalytic activity. Heating the sample before testing decreased the enzyme in the film by about 30% but did not eliminate it completely. The results of the activity test of two samples are summarized in Table 1 together with reference values for a spontaneous reaction without enzyme. It is necessary to underline that enzymatic activity on spherical supports was higher than the respective value in flat films, which could indicate that apparent catalytic efficiency was improved due to an increased area-to-volume ratio. 

The catalytic efficiency of an enzyme is usually expressed by the ratio of its rate constant or turnover number (moles of substrate reacted per mol of... 

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