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      Directed Evolution: Bringing New Chemistry to Life

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          Abstract

          Tailor‐made: Discussed herein is the ability to adapt biology's mechanisms for innovation and optimization to solving problems in chemistry and engineering. The evolution of nature's enzymes can lead to the discovery of new reactivity, transformations not known in biology, and reactivity inaccessible by small‐molecule catalysts.

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          Most cited references20

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          Exploring protein fitness landscapes by directed evolution.

          Directed evolution circumvents our profound ignorance of how a protein's sequence encodes its function by using iterative rounds of random mutation and artificial selection to discover new and useful proteins. Proteins can be tuned to adapt to new functions or environments by simple adaptive walks involving small numbers of mutations. Directed evolution studies have shown how rapidly some proteins can evolve under strong selection pressures and, because the entire 'fossil record' of evolutionary intermediates is available for detailed study, they have provided new insight into the relationship between sequence and function. Directed evolution has also shown how mutations that are functionally neutral can set the stage for further adaptation.
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            Directed evolution of cytochrome c for carbon-silicon bond formation: Bringing silicon to life.

            Enzymes that catalyze carbon-silicon bond formation are unknown in nature, despite the natural abundance of both elements. Such enzymes would expand the catalytic repertoire of biology, enabling living systems to access chemical space previously only open to synthetic chemistry. We have discovered that heme proteins catalyze the formation of organosilicon compounds under physiological conditions via carbene insertion into silicon-hydrogen bonds. The reaction proceeds both in vitro and in vivo, accommodating a broad range of substrates with high chemo- and enantioselectivity. Using directed evolution, we enhanced the catalytic function of cytochrome c from Rhodothermus marinus to achieve more than 15-fold higher turnover than state-of-the-art synthetic catalysts. This carbon-silicon bond-forming biocatalyst offers an environmentally friendly and highly efficient route to producing enantiopure organosilicon molecules.
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              Catalytic promiscuity and the evolution of new enzymatic activities.

              Several contemporary enzymes catalyze alternative reactions distinct from their normal biological reactions. In some cases the alternative reaction is similar to a reaction that is efficiently catalyzed by an evolutionary related enzyme. Alternative activities could have played an important role in the diversification of enzymes by providing a duplicated gene a head start towards being captured by adaptive evolution.
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                Author and article information

                Contributors
                frances@cheme.caltech.edu , http://fhalab.caltech.edu
                Journal
                Angew Chem Int Ed Engl
                Angew. Chem. Int. Ed. Engl
                10.1002/(ISSN)1521-3773
                ANIE
                Angewandte Chemie (International Ed. in English)
                John Wiley and Sons Inc. (Hoboken )
                1433-7851
                1521-3773
                28 November 2017
                09 April 2018
                : 57
                : 16 , 350 Years of Merck KGaA, Darmstadt, Germany ( doiID: 10.1002/anie.v57.16 )
                : 4143-4148
                Affiliations
                [ 1 ] Division of Chemistry and Chemical Engineering California Institute of Technology 210-41 1200 E. California Blvd. Pasadena CA 91125 USA
                Author information
                http://orcid.org/0000-0002-4027-364X
                Article
                ANIE201708408
                10.1002/anie.201708408
                5901037
                29064156
                46d3b141-369f-440e-b2a0-d5cad4cd1772
                © 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.

                This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.

                History
                : 15 August 2017
                Page count
                Figures: 5, Tables: 0, References: 17, Pages: 6, Words: 0
                Funding
                Funded by: National Science Foundation
                Award ID: MCB-1513007
                Funded by: California Institute of Technology
                Award ID: Resnick Sustainability Institute
                Award ID: CI2 Innovation Program
                Categories
                Essay
                Essays
                Biocatalysis
                Custom metadata
                2.0
                anie201708408
                April 9, 2018
                Converter:WILEY_ML3GV2_TO_NLMPMC version:version=5.3.4 mode:remove_FC converted:16.04.2018

                Chemistry
                biocatalysis,enzymes,heme proteins,protein engineering,synthetic methods
                Chemistry
                biocatalysis, enzymes, heme proteins, protein engineering, synthetic methods

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