Enzyme mimic (orArtificial enzyme) is a branch of biomimetic chemistry, which aims at imitating the function of natural enzymes.[1][2][3][4][5] Anenzyme mimic is asmall molecule complex that models the molecular structure, spectroscopic properties, or reactivity of anenzyme, sometimes called bioinspired complexes.[6]
Enzymes are biological catalysts: biopolymers thatcatalyze areaction. Although a small number of natural enzymes are built fromRNA–termedRibozymes–most enzymes areproteins. Like any other protein, an enzyme is anamino acidpolymer with addedcofactors and otherpost-translational modifications. Often, most of the amino acid polymer is indirectly involved with the enzymes function, perhaps providing ancillary structure or connectivity, indirect activity regulation, or molecular identification of the enzyme. As a result, most enzymes are large molecules weighing manykilodaltons. This bulk can obscure various investigative techniques such asNMR,EPR,electrochemistry,crystallography, among others. It is standard practice to compare spectroscopic data from enzymes to similar spectroscopic data derived from better characterized small molecules. In this way, the understanding of metalloenzymes and othermetalloproteins have developed. In many cases, the small molecule analogs were created for other reasons; however, it has been increasingly common for groups to intentionally make small molecule analogs also known as enzyme mimics. These enzyme mimics are prime examples ofbioinorganic chemistry.
Most enzyme mimic studies are motivated by a combination of factors, including factors that are unrelated to the enzyme. Several of the factors that are related to the enzyme are listed below.
Defining the active site structure. A number of important active sites are still poorly defined. This includes theoxygen evolving complex andnitrogenase. In an effort to understand these enzymes, small molecule analogs are created and compared to the data which exists for the proteins.
Understanding the active site function. The structure of some enzymes are very well characterized, however, the function of some component of the active site is poorly understood. This is often investigated throughsite-directed mutagenesis. In addition, the synthesis of a model complex can suggest the function of various components.
Reproducing the enzymes function. A number of enzymes are an interest since they catalyze a reaction chemist find challenging. These reactions include the partial oxidation of a hydrocarbon bymethane monooxygenase (MMO) or the oxidation and production ofhydrogen byhydrogenase. "Functional" enzyme mimics or bioinspired catalysts are designed with characteristics of the enzyme in hopes of reproducing the enzymes functionality.
This list is extremely abbreviated in terms of the enzymes mimicked and the primary investigators working on each enzyme mimic.
Richard Holm's work on mimics ofnitrogenase and creation ofiron sulfur clusters.
Stephen Lippard's work onMMO.
Thomas Rauchfuss's, Marcetta Darensbourg's and Christopher Pickett's work onHydrogenase mimics.
Harry Gray's work withporphyrins complexes.
Ronald Breslow and Larry E. Overman coined the term of "artificial enzyme".[3]
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