Nicholas Turner (chemist)

Last updated
Nicholas Turner
FRS
Born
Nicholas John Turner

1959or1960(age 64–65) [1]
Alma mater University of Bristol [2]
University of Oxford [2]
Known for Biotechnology
Cell biology
Biocatalysis
Organic synthesis
Awards
Scientific career
Fields Biochemistry
Organic chemistry
InstitutionsThe University of Manchester
Thesis Mechanistic studies on isopenicillin N synthase  (1985)
Doctoral advisor Jack Baldwin

Nicholas John Turner, FRS is a British chemist and a Professor in the Department of Chemistry at The University of Manchester. [2] His research in general is based on biochemistry and organic chemistry, specifically on biotechnology, cell biology, biocatalysis and organic synthesis. [9] [10]

Contents

Education

Turner completed his Bachelor of Science degree in Chemistry in 1982 at University of Bristol. [2] He then read for his Doctor of Philosophy degree at University of Oxford on Mechanistic studies on isopenicillin N synthase and successfully completed it in 1985. [11] His PhD was supervised by Jack Baldwin. [11]

Research and career

Upon completing his PhD, Turner spent two years (1985 - 1987) with George M. Whitesides at Harvard University as a Royal Society Junior Research Fellow. [2] [12] He then moved to University of Exeter as a Lecturer in 1987, before moving to University of Edinburgh for the position of Reader in 1995. [12] He was promoted to the position of Professor in 1998 and moved to University of Manchester as a Professor of Chemical Biology in 2004.

Turner's research in general is based on biochemistry and organic chemistry, specifically on biotechnology, cell biology, biocatalysis and organic synthesis. [9] [10]

Turner is the Director of CoEBio3, an organization designed to provide scientific environment in which the necessary research and development can be carried out to create new biocatalyst-based processes to meet the changing needs of industry in the next 10–20 years. [13] He is also the Co-founder of Ingenza and Co-director of SYNBIOCHEM. [14] [15] Turner is also the author of several books in the field of biocatalysis including Introduction to Biocatalysis Using Enzymes and Microorganisms, [16] and Biocatalysis in Organic Synthesis: The Retrosynthesis Approach. [17]

Notable work

Turner was elected as a Fellow of the Royal Society in the year 2020. [8] Regarded one of the world's leading researchers [8] in the field of Biocatalysis, his profile reads:

"Nicholas Turner undertakes research focussed on creating new enzymes for application as biocatalysts for chemical synthesis. [18] [19] [20] His group combine enzyme discovery with protein engineering and directed evolution methods in order to develop biocatalysts with tailored properties including high (stereo)selectivity, improved activity and enhanced stability. These biocatalysts, which include amine/alcohol oxidases, imine reductases, lyases, transaminases and monooxygenases, are then applied to the synthesis of a range of target molecules especially pharmaceuticals and fine chemicals. [21] [22] ... Nick also has a passion for promoting the wider application of biocatalysis across the entire chemical community and has developed guidelines for 'biocatalytic retrosynthesis' [17] to encourage greater adoption of biocatalysis amongst synthetic chemists."

Awards and nominations

Major publications

Related Research Articles

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<span class="mw-page-title-main">Tropinone</span> Chemical compound

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Reductive amination is a form of amination that involves the conversion of a carbonyl group to an amine via an intermediate imine. The carbonyl group is most commonly a ketone or an aldehyde. It is a common method to make amines and is widely used in green chemistry since it can be done catalytically in one-pot under mild conditions. In biochemistry, dehydrogenase enzymes use reductive amination to produce the amino acid, glutamate. Additionally, there is ongoing research on alternative synthesis mechanisms with various metal catalysts which allow the reaction to be less energy taxing, and require milder reaction conditions. Investigation into biocatalysts, such as imine reductases, have allowed for higher selectivity in the reduction of chiral amines which is an important factor in pharmaceutical synthesis.

The Baeyer–Villiger oxidation is an organic reaction that forms an ester from a ketone or a lactone from a cyclic ketone, using peroxyacids or peroxides as the oxidant. The reaction is named after Adolf von Baeyer and Victor Villiger who first reported the reaction in 1899.

<span class="mw-page-title-main">Biocatalysis</span> Use of natural catalysts to perform chemical transformations

Biocatalysis refers to the use of living (biological) systems or their parts to speed up (catalyze) chemical reactions. In biocatalytic processes, natural catalysts, such as enzymes, perform chemical transformations on organic compounds. Both enzymes that have been more or less isolated and enzymes still residing inside living cells are employed for this task. Modern biotechnology, specifically directed evolution, has made the production of modified or non-natural enzymes possible. This has enabled the development of enzymes that can catalyze novel small molecule transformations that may be difficult or impossible using classical synthetic organic chemistry. Utilizing natural or modified enzymes to perform organic synthesis is termed chemoenzymatic synthesis; the reactions performed by the enzyme are classified as chemoenzymatic reactions.

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<span class="mw-page-title-main">Nigel Scrutton</span> British biochemist (born 1964)

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Morphinone reductase is an enzyme which catalyzes the NADH-dependent saturation of the carbon-carbon double bond of morphinone and codeinone, yielding hydromorphone and hydrocodone respectively. This saturation reaction is assisted by a FMN cofactor and the enzyme is a member of the α/β-barrel flavoprotein family. The sequence of the enzyme has been obtained from bacteria Pseudomonas putida M10 and has been successfully expressed in yeast and other bacterial species. The enzyme is reported to harbor high sequence and structural similarity to the Old Yellow Enzyme, a large group of flavin-dependent redox biocatalysts of yeast species, and an oestrogen-binding protein of Candida albicans. The enzyme has demonstrated value in biosynthesis of semi-opiate drugs in microorganisms, expanding the chemical diversity of BIA biosynthesis.

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<span class="mw-page-title-main">Imine reductase</span> Industrially relevant enzyme

An imine reductase (IRED) is an enzyme that reduces imines to amines. This family of enzymes is employed in the industrial production of amine-containing pharmaceuticals. The IRED enzymes that are found to catalyze both imine formation and imine reduction are called reductive aminases (RedAms).

References

  1. "Prof. Nicholas Turner (CV)" (PDF). Retrieved 18 June 2020.
  2. 1 2 3 4 5 Turner Lab. "Prof. Nicholas Turner" . Retrieved 18 June 2020.
  3. 1 2 Royal Society of Chemistry. "Dextra Carbohydrate Chemistry Award" . Retrieved 18 June 2020.
  4. 1 2 Royal Society of Chemistry. "Corday-Morgan Prize Previous Winners" . Retrieved 18 June 2020.
  5. 1 2 Royal Society of Chemistry. "Organic Industrial Chemistry Award 2009 winner" . Retrieved 18 June 2020.
  6. 1 2 Royal Society of Chemistry. "Organic Stereochemistry Award 2017 Winner" . Retrieved 18 June 2020.
  7. 1 2 American Chemical Society. "Congratulations to the 2018 ACS Catalysis Lectureship Recipient: Professor Nicholas Turner" . Retrieved 18 June 2020.
  8. 1 2 3 4 Royal Society. "Royal Society Fellows" . Retrieved 18 June 2020.
  9. 1 2 "Prof. Nicholas J. Turner: Publications" . Retrieved 18 June 2020.
  10. 1 2 "Prof. Nicholas J. Turner: Publications" . Retrieved 16 June 2020.
  11. 1 2 Nicholas J., Turner (1985). Mechanistic studies on isopenicillin N synthase (PhD thesis).(subscription required)
  12. 1 2 University of Manchester NMR Group. "Prof. Nicholas Turner" . Retrieved 18 June 2020.
  13. CoEBio3. "CoEBio3 Activities" . Retrieved 18 June 2020.{{cite web}}: CS1 maint: numeric names: authors list (link)
  14. Ingenza. "Ingenza(Management)" . Retrieved 18 June 2020.
  15. (Synbiochem) Manchester Synthetic Biology Research Center. "Synbiochem" . Retrieved 18 June 2020.
  16. Turner, Nicholas; Turner, Michael K.; Roberts, Stanley M.; Willetts, Andrew J. (27 January 1995). Willetts, Andrew J. (ed.). Introduction to Biocatalysis Using Enzymes and Microorganisms. Cambridge: Cambridge University Press. doi:10.1017/CBO9780511752254. ISBN   9780511752254.
  17. 1 2 Turner, Nicholas; Humphreys, Luke (8 February 2018). Biocatalysis in Organic Synthesis: The Retrosynthesis Approach. United Kingdom: Royal Society of Chemistry. ISBN   978-1-78801-342-0.
  18. Turner, Nicholas (23 April 2012). "Oxidation of C - N Bonds". In Drauz, Karlheinz; Gröger, Harald; May, Oliver (eds.). Biocatalysis in Organic Synthesis: The Retrosynthesis Approach. United Kingdom: Wiley‐VCH Verlag GmbH & Co. KGaA. pp. 1535–1552. doi:10.1002/9783527639861. ISBN   9783527325474.
  19. Turner, Nicholas; O’Reilly, Elaine (2013). "Biocatalytic retrosynthesis" (PDF). Nature Chemical Biology. 9 (5): 285–288. doi:10.1038/nchembio.1235. PMID   23594772 . Retrieved 18 June 2020.
  20. Turner, Nicholas (2009). "Directed evolution drives the next generation of biocatalysts". Nature Chemical Biology. 5 (8): 567–573. doi:10.1038/nchembio.203. PMID   19620998 . Retrieved 18 June 2020.
  21. Turner, Nicholas; Jones, Patrik R.; Akhtar, M. Kalim (2012). "Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities". PNAS. 110 (1): 87–92. doi: 10.1073/pnas.1216516110 . PMC   3538209 . PMID   23248280.
  22. Turner, N.; Köhler, V.; Wilson, V.M.; Dürrenberger, M.; Ghislieri, D.; Churakova, E.; Quinto, T; Knörr, L.; Häussinger, D.; Hollmann, F.; Ward, T.R. (2013). "Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes". Nature Chemistry. 5 (2): 93–99. doi:10.1038/nchem.1498. PMID   23344429. S2CID   205290846 . Retrieved 18 June 2020.