Editorial Cite This: ACS Catal. 2018, 8, 1601−1601
pubs.acs.org/acscatalysis
Nicholas Turner Selected To Deliver the Seventh ACS Catalysis Lectureship
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originate from his lab, such as his team’s recent discovery of an NADP(H)-dependent reductive aminase from Aspergillus oryzae that promotes the reductive coupling of a broad set of carbonyl compounds with a variety of primary and secondary amines with up to >98% conversion and with up to >98% enantiomeric excess.14 Prof. Nicholas Turner’s contributions to catalysis science and technology have significantly changed the way researchers think about the field. ACS Catalysis is pleased that he was selected as the first Lectureship honoree representing the fields of biocatalysis and enzymology, and we eagerly anticipate his award symposium at ACS in Boston!
rofessor Nicholas J. Turner of the University of Manchester, U.K., has been selected to deliver the 2018 ACS Catalysis Lectureship for the Advancement of Catalytic Science, cosponsored by the ACS Division of Catalysis Science and Technology and ACS Catalysis, at the 256th ACS National Meeting in Boston, MA. Prof. Turner, director of the Centre of Excellence for Biocatalysis, Biotransformations and Biocatalytic Manufacture (CoEBio3) in the U.K., is one of the world’s leading scientists in the engineering of enzymes for application as biocatalysts in chemical synthesis. His research contributions successfully demonstrate that a wide range of different enzymes can be used to catalyze highly selective transformations that are of importance to both academic and industrial chemists. Moreover, he has applied these engineered biocatalysts in processes that result in the enantioselective production of relevant target molecules including pharmaceuticals, specialty chemicals, and biofuels. The ACS Catalysis Lectureship focuses on achievements in the 7 years prior to the award, or in this year’s case, the period from 2010 to 2017. Of course, many of the new achievements in this period build off prior pioneering work in earlier eras. In 2002, Prof. Turner coauthored an early paper applying directed evolution methods to create new biocatalysts for enantioselective amine oxidation.1 This early work ultimately led to the creation of a start-up company, Ingenza Ltd.,2 as well as several highly cited papers on enzymatic amine oxidation.3−5 His research group has used such engineered biocatalysts to develop a more efficient process for the manufacture of the hepatitis C drug telaprevir,6 and they have introduced high throughput screening methods that allow the identification of the best catalyst in large libraries of protein variants.7,8 These methods have been adopted and exploited by other groups around the world. His team has applied the concept of directed evolution of enzymes to a diverse range of different biocatalysts including amine/alcohol/amino acid oxidases, P450 monooxygenases, imine reductases, ammonia lyases, and transaminases, among others. In recent years, he has begun to explore synthetic biology approaches for the creation of improved biocatalysts in which multiple genes are coexpressed in microbial hosts to create cell factories capable of multistep transformations. This approach has been applied to the conversion of renewable feedstock fatty acids into long-chain alcohols and alkanes.9 He has also developed cascade processes involving combinations of biocatalysts with chemo-catalysts and synthetic enzymes, including landmark papers reporting the first example of asymmetric hydrogen borrowing involving amine dehydrogenases for conversion of alcohols to amines10 and the combination of biocatalysts with an artificial transfer hydrogenase.11 Turner has additionally published 10 papers in ACS Catalysis to date, with his first appearing in the inaugural volume of the journal, in 2011,12 and a recent example identified by ISI Web of Science as a highly cited paper (top 1% most cited).13 New discoveries appearing in other high profile journals continue to © 2018 American Chemical Society
Christopher W. Jones, Editor-in-Chief
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Georgia Institute of Technology
AUTHOR INFORMATION
Notes
Views expressed in this editorial are those of the author and not necessarily the views of the ACS.
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REFERENCES
(1) Alexeeva, M.; Enright, A.; Dawson, M. J.; Mahmoudian, M.; Turner, N. J. Angew. Chem., Int. Ed. 2002, 41, 3177. (2) Ingenza website homepage. www.ingenza.com. (3) Schrittwieser, J. H.; Groenendaal, B.; Resch, V.; Ghislieri, D.; Wallner, S.; Fischereder, E. M.; Fuchs, E.; Grischek, B.; Sattler, J. H.; Macheroux, P.; Turner, N. J.; Kroutil, W. Angew. Chem., Int. Ed. 2014, 53, 3731. (4) O’Reilly, E.; Iglesias, C.; Ghislieri, D.; Hopwood, J.; Galman, J. L.; Lloyd, R. C.; Turner, N. J. Angew. Chem., Int. Ed. 2014, 53, 2447. (5) Ghislieri, D.; Green, A. P.; Pontini, M.; Willies, S. C.; Rowles, I.; Frank, A.; Grogan, G.; Turner, N. J. J. Am. Chem. Soc. 2013, 135, 10863. (6) Znabet, A.; Polak, M. M.; Janssen, E.; de Kanter, F. J. J.; Turner, N. J.; Orru, R. V. A.; Ruijter, E. Chem. Commun. 2010, 46, 7918. (7) Green, A. P.; Turner, N. J.; O’Reilly, E. Angew. Chem., Int. Ed. 2014, 53, 10714. (8) Moore, B. D.; Stevenson, L.; Watt, A.; Flitsch, S.; Turner, N. J.; Cassidy, C.; Graham, D. Nat. Biotechnol. 2004, 22, 1133. (9) Akhtar, M. K.; Turner, N. J.; Jones, P. R. Proc. Natl. Acad. Sci. U. S. A. 2013, 110, 87. (10) Mutti, F. G.; Knaus, T.; Scrutton, N. S.; Breuer, M.; Turner, N. J. Science 2015, 349, 1525. (11) Kohler, V.; Wilson, Y. M.; Durrenberger, M.; Ghislieri, D.; Churakova, E.; Quinto, T.; Knorr, L.; Haussinger, D.; Hollmann, F.; Turner, N. J.; Ward, T. R. Nat. Chem. 2013, 5, 93. (12) O’Neill, M.; Hauer, B.; Schneider, N.; Turner, N. J. ACS Catal. 2011, 1, 1014−1016. (13) France, S. P.; Hepworth, L. J.; Turner, N. J.; Flitsch, S. L. ACS Catal. 2017, 7, 710−724. (14) Aleku, G. A.; France, S. P.; Man, H.; Mangas-Sanchez, J.; Montgomery, S. L.; Sharma, M.; Leipold, F.; Hussain, S.; Grogan, G.; Turner, N. J. Nat. Chem. 2017, 9, 961−969.
Published: February 2, 2018 1601
DOI: 10.1021/acscatal.8b00261 ACS Catal. 2018, 8, 1601−1601
