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  Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coil's Periplasm

Zhao, J., Rebelein, J. G., Mallin, H., Trindler, C., Pellizzoni, M. M., & Ward, T. R. (2018). Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coil's Periplasm. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 140(41), 13171-13175. doi:10.1021/jacs.8b07189.

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 Creators:
Zhao, Jingming1, Author
Rebelein, Johannes G.2, Author                 
Mallin, Hendrik1, Author
Trindler, Christian1, Author
Pellizzoni, Michela M.1, Author
Ward, Thomas R.1, Author
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1external, ou_persistent22              
2University of Basel, ou_persistent22              

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 Abstract: Artificial metalloenzymes (ArMs), which combine an abiotic metal cofactor with a protein scaffold, catalyze various synthetically useful transformations. To complement the natural enzymes' repertoire, effective optimization protocols to improve ArM's performance are required. Here we report on our efforts to optimize the activity of an artificial transfer hydrogenase (ATHase) using Escherichia coli whole cells. For this purpose, we rely on a self-immolative quinolinium substrate which, upon reduction, releases fluorescent umbelliferone, thus allowing efficient screening. Introduction of a loop in the immediate proximity of the Ir-cofactor afforded an ArM with up to 5-fold increase in transfer hydrogenation activity compared to the wild-type ATHase using purified mutants.

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 Dates: 2018
 Publication Status: Issued
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 Identifiers: ISI: 000447953600009
DOI: 10.1021/jacs.8b07189
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Title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Source Genre: Journal
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Pages: - Volume / Issue: 140 (41) Sequence Number: - Start / End Page: 13171 - 13175 Identifier: ISSN: 0002-7863