Artificial concurrent catalytic processes involving enzymes. Issue 3 (28th October 2014)
- Record Type:
- Journal Article
- Title:
- Artificial concurrent catalytic processes involving enzymes. Issue 3 (28th October 2014)
- Main Title:
- Artificial concurrent catalytic processes involving enzymes
- Authors:
- Köhler, Valentin
Turner, Nicholas J. - Abstract:
- Abstract : Various aspects of simultaneous enzymatic catalysis are reviewed with an emphasis on the combination of biocatalysts with transition metal catalysts. Abstract : The concurrent operation of multiple catalysts can lead to enhanced reaction features including (i) simultaneous linear multi-step transformations in a single reaction flask (ii) the control of intermediate equilibria (iii) stereoconvergent transformations (iv) rapid processing of labile reaction products. Enzymes occupy a prominent position for the development of such processes, due to their high potential compatibility with other biocatalysts. Genes for different enzymes can be co-expressed to reconstruct natural or construct artificial pathways and applied in the form of engineered whole cell biocatalysts to carry out complex transformations or, alternatively, the enzymes can be combined in vitro after isolation. Moreover, enzyme variants provide a wider substrate scope for a given reaction and often display altered selectivities and specificities. Man-made transition metal catalysts and engineered or artificial metalloenzymes also widen the range of reactivities and catalysed reactions that are potentially employable. Cascades for simultaneous cofactor or co-substrate regeneration or co-product removal are now firmly established. Many applications of more ambitious concurrent cascade catalysis are only just beginning to appear in the literature. The current review presents some of the most recentAbstract : Various aspects of simultaneous enzymatic catalysis are reviewed with an emphasis on the combination of biocatalysts with transition metal catalysts. Abstract : The concurrent operation of multiple catalysts can lead to enhanced reaction features including (i) simultaneous linear multi-step transformations in a single reaction flask (ii) the control of intermediate equilibria (iii) stereoconvergent transformations (iv) rapid processing of labile reaction products. Enzymes occupy a prominent position for the development of such processes, due to their high potential compatibility with other biocatalysts. Genes for different enzymes can be co-expressed to reconstruct natural or construct artificial pathways and applied in the form of engineered whole cell biocatalysts to carry out complex transformations or, alternatively, the enzymes can be combined in vitro after isolation. Moreover, enzyme variants provide a wider substrate scope for a given reaction and often display altered selectivities and specificities. Man-made transition metal catalysts and engineered or artificial metalloenzymes also widen the range of reactivities and catalysed reactions that are potentially employable. Cascades for simultaneous cofactor or co-substrate regeneration or co-product removal are now firmly established. Many applications of more ambitious concurrent cascade catalysis are only just beginning to appear in the literature. The current review presents some of the most recent examples, with an emphasis on the combination of transition metal with enzymatic catalysis and aims to encourage researchers to contribute to this emerging field. … (more)
- Is Part Of:
- Chemical communications. Volume 51:Issue 3(2015)
- Journal:
- Chemical communications
- Issue:
- Volume 51:Issue 3(2015)
- Issue Display:
- Volume 51, Issue 3 (2015)
- Year:
- 2015
- Volume:
- 51
- Issue:
- 3
- Issue Sort Value:
- 2015-0051-0003-0000
- Page Start:
- 450
- Page End:
- 464
- Publication Date:
- 2014-10-28
- Subjects:
- Chemistry -- Periodicals
540 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/cc ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c4cc07277d ↗
- Languages:
- English
- ISSNs:
- 1359-7345
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3139.350000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 922.xml