A cell-penetrating artificial metalloenzyme regulates a gene switch in a designer mammalian cell

Autor: Yasunori Okamoto, Ryosuke Kojima, Fabian Schwizer, Eline Bartolami, Tillmann Heinisch, Stefan Matile, Martin Fussenegger, Thomas R. Ward

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)

Artificial enzymes can be used to elicit reactions in cells. Here, the authors developed such an artificial catalyst combined with a genetic switch, and showed that it was readily taken up by human cells and able to kick off a reaction cascade result

Externí odkaz: https://doaj.org/article/a6bc18d7dfce4b7480d201ebe6f6f857

Chimeric streptavidins as host proteins for artificial metalloenzymes

Autor: Michela M. Pellizzoni, Christopher W. Wood, Valerio Sabatino, Thomas R. Ward, Derek N. Woolfson, Stefan Matile, Yoann Cotelle, Fabian Schwizer

Publikováno v: Pellizzoni, M M, Schwizer, F, Wood, C W, Sabatino, V, Cotelle, Y, Matile, S, Woolfson, D N & Ward, T R 2018, ' Chimeric streptavidins as host proteins for artificial metalloenzymes ', ACS Catalysis, vol. 8, no. 2, pp. 1476-1484 . https://doi.org/10.1021/acscatal.7b03773
ACS Catalysis
ACS Catalysis, 2018, 8 (2), pp.1476-1484. ⟨10.1021/acscatal.7b03773⟩
Pellizzoni, M M, Schwizer, F, Wood, C W, Sabatino, V, Cotelle, Y, Matile, S, Woolfson, D N & Ward, T R 2018, ' Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes ', ACS Catalysis, vol. 8, no. 2, pp. 1476-1484 . https://doi.org/10.1021/acscatal.7b03773
ACS Catalysis, American Chemical Society, 2018, 8 (2), pp.1476-1484. ⟨10.1021/acscatal.7b03773⟩
ACS Catalysis, Vol. 8, No 1 (2018) pp. 1476-1484

© 2018 American Chemical Society. The streptavidin scaffold was expanded with well-structured naturally occurring motifs. These chimeric scaffolds were tested as hosts for biotinylated catalysts as artificial metalloenzymes (ArM) for asymmetric tran

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94cb31a7df8edf6d19fc650d27c45a4a
https://hdl.handle.net/20.500.11820/6c94f1f8-dbef-415a-82ab-ddbc1373bf2b

Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

Autor: Yasunori Okamoto, Tillmann Heinisch, Yifan Gu, Vincent Lebrun, Michela M. Pellizzoni, Fabian Schwizer, Valentin Köhler, Thomas R. Ward, Jared C. Lewis, Raphael Reuter

Publikováno v: Chemical reviews. 118(1)

The incorporation of a synthetic, catalytically competent metallocofactor into a protein scaffold to generate an artificial metalloenzyme (ArM) has been explored since the late 1970’s. Progress in the ensuing years was limited by the tools availabl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a39a0caed364d7a10e0ec42aa5232c51
https://pubmed.ncbi.nlm.nih.gov/28714313

Correction: E. coli surface display of streptavidin for directed evolution of an allylic deallylase

Autor: Tillmann Heinisch, Vitor B. Pinheiro, Markus Jeschek, Sven Panke, Thomas R. Ward, Eszter Csibra, Brett Garabedian, Jaicy Vallapurackal, Fabian Schwizer, Philippe Marlière

Publikováno v: Chemical Science

Correction for ‘E. coli surface display of streptavidin for directed evolution of an allylic deallylase’ by Tillmann Heinisch et al., Chem. Sci., 2018, 9, 5383–5388.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::430b173ecefbd5257597bd417a500a9a
https://doi.org/10.1039/c9sc90139f

Light-driven electron injection from a biotinylated triarylamine donor to [Ru(diimine)3](2+)-labeled streptavidin

Autor: Thomas R. Ward, Juliane Klehr, Fabian Schwizer, Andrea Pannwitz, Oliver S. Wenger, Sascha G. Keller

Publikováno v: Organicbiomolecular chemistry. 14(30)

Electron transfer from a biotinylated electron donor to photochemically generated Ru(III) complexes covalently anchored to streptavidin is demonstrated by means of time-resolved laser spectroscopy. Through site-selective mutagenesis, a single cystein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c7d7ff4b4af1dafaf2adb2cd050e5fa
https://pubmed.ncbi.nlm.nih.gov/27411288