Enzyme catalysis biomimetic

Popovitz-Biro, R. Chang, H. C. Tang, C. P. Shochet, N. Lahav, M. Leiserowitz, L. In Chemical Approaches to Understanding Enzyme Catalysis Biomimetic Chemistry and Transition-State Analogs Green, B. S. Ashani, Y. Chipman, D., Eds. Elsevier Amsterdam, 1982, pp. 88-105. 

Chemical Approaches to Understanding Enzyme Catalysis Biomimetic Chemistry and Transition-State Analogs edited by B.S. Green, Y. Ashani and D.Chipman... 

Warshel, A., Russell, S.T., and Weiss, R.M (1982) in B.S. Green, Y. Ashani, and D. Chipman, (eds.), Chemical Approaches to Understanding Enzyme Catalysis Biomimetic Chemistry and Transition-State Analogs, Elsevier, Amsterdam, 267. 

In this chapter we summarize key molecular concepts in biocatalysis and compare them with the molecular understanding of reaction mechanisms in heterogeneous catalysis that was developed in the previous chapters. The first four sections of this chapter emphasize enzyme catalysis. Biomimetic approaches are described in later sections. 

See for example the pioneering work of Breslow Bres-low, R. Dong, S. D. Biomimetic Reactions Catalyzed by Cyclodextrins and their Derivatives Chem. Rev. 1998, 98,1997-2011 and Breslow, R. Biomimetic Chemistiy and Artificial Enzymes - Catalysis by Design Acc Chem. Res. 1995,28,146-153. 

Breslow, R. (1995) Biomimetic chemistry and artifical enzymes -catalysis hy design. Acc. Chem. Res.. 28. 146-153. 

The area between enzymatic and chemical catalyses, associated with simulation of biochemical processes by their basic parameters, is accepted as mimetic catalysis. The key aspect of the mimetic catalyst is diversity of enzyme and biomimetic function processes, which principally distinguishes the mimetic model from traditional full simulation. Based on the analysis of conformities and diversities of enzymatic and chemical catalysis, the general aspects of mimetic catalysis are discussed. An idealized model of the biomimetic catalyst and the exclusive role of the membrane in its structural organization are considered. The most important achievements in the branch of catalysis are shown, in particular, new approaches to synthesis and study of biomimetic catalase, peroxidase and monooxidases reactions. 

New Trends in Enzyme Catalysis and Biomimetic Chemical Reactions... 

Breslow R. Biomimetic chemistry and artificial enzymes catalysis by design. Accts. Chem. Res. 1995 28 146-153. 

A wide range of chemical compounds have been imprinted successfully, ranging from small molecules,40 2 to large proteins and cells.43 MIPs have been developed for a variety of applications including chromatography,4445 solid-phase extraction (SPE),46 47 enzyme catalysis,48 sensor technology,44>49>50 biomimetic sensors,5153 and immunoassays.54-56 MIPs are robust, inexpensive and, in many cases, possess affinity and specificity that are suitable for industrial applications. The high specificity and... 

Likhtenshtein, G.l. (2003) New Trends in Enzyme Catalysis and Biomimetic Chemical Reactions, Kluwer Academic Publishers, Springer. 

These advances can collectively be viewed as the growing field of biocatalysis and biomimetics. Along with the biotechnical developments, these provide another option for exploiting the potential of enzyme catalysis in the chemicals industry. The following chapters present representative examples of current advances in this emerging field. 

Breslow, R (1995). Biomimetic chemistry and artificial enzymes Catalysis by design. Accounts of Chemical Research, 28(3), 146-153. 

All the preceding substrates, even oxyheme, are expected to form carbanions readily. In fact, under solution conditions, in a mixture of f-butanol, dimethylformamide and base, the indole and flavonol derivatives undero oxygenation biomimetically to cleave the C-2, C-3 bond. Like indole itself, the C-3-substituted indoles, on enzymic catalysis, are structurally pre-disposed to yield tetrahedral carbanionic centers at C-3, suitably soft for easy and efficient addition to triplet dioxygen 139). The resulting peroxide (53) (Scheme 24) could possibly cleave its C-2, C-3 bond by the expedient of hydration (54) followed by cleavage to the keto-aldehyde (55). 

What has been described as biomimetic control of chemical selectivity is already possible. When the steroid 3a-cholestanol is esterified with 4-iodophenylacetic acid and treated with chlorine in the dark the iododichloride can generate free radicals which attack the C-17 of the steroid. The shorter ester derived from benzoic acid attacks C-9 (Figure 6.33). In another context metal porphyrin complexes have been devised which can hydroxylate hydrocarbons (Figure 6.34). Many more ideas of this kind are likely to follow a better understanding of the mechanisms of enzyme catalysis. 

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