Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Tillmann Heinisch"'
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
Autor:
Tsvetan Kardashliev, Tillmann Heinisch, Jaicy Vallapurackal, Fabian Schwizer, Sven Panke, Thomas R. Ward, Martin Held, Alain Baiyoumy
Publikováno v:
ACS Catalysis, 11 (17)
ACS Catalysis
ACS Catalysis
Artificial metalloenzymes (ArMs) combine characteristics of both homogeneous catalysts and enzymes. Merging abiotic and biotic features allows for the implementation of new-to-nature reactions in living organisms. Here, we present the directed evolut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e894a60c545ebbf4cdccc0f5d25bec4b
https://hdl.handle.net/20.500.11850/506507
https://hdl.handle.net/20.500.11850/506507
Autor:
Jan Kern, Aaron S. Brewster, In-Sik Kim, Sheraz Gul, Alexander Batyuk, Kyle D. Sutherlin, Asmit Bhowmick, Tillmann Heinisch, Andrew S. Borovik, Thomas R. Ward, Franklin D. Fuller, Jonathan D Paretsky, Alec H. Follmer, Kelsey R. Miller, Michael Green, Kaustuv Mittra, Nicholas K. Sauter, Junko Yano
Publikováno v:
Inorg Chem
Inorganic chemistry, vol 59, iss 9
Inorganic chemistry, vol 59, iss 9
An important class of non-heme dioxygenases contains a conserved Fe binding site that consists of a 2-His-1-carboxylate facial triad. Results from structural biology show that, in the resting state, these proteins are six-coordinate with aqua ligands
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6bdb831c29fc28e72a3c3855c0aa963
https://europepmc.org/articles/PMC7219546/
https://europepmc.org/articles/PMC7219546/
Publikováno v:
Chemical communications (Cambridge, England), vol 54, iss 35
Secondary coordination spheres of metal complexes are instrumental in controlling properties that are linked to function. To study these effects in aqueous solutions artificial Cu proteins have been developed using biotin–streptavidin (Sav) technol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58e29a7de530b1d48119ca1642c906a5
https://escholarship.org/uc/item/4xd2266r
https://escholarship.org/uc/item/4xd2266r
Publikováno v:
Dalton Transactions
Ferritin, a naturally occuring iron-storage protein, plays an important role in nanoengineering and biomedical applications. Upon iron removal, apoferritin was shown to allow the encapsulation of an artificial transfer hydrogenase (ATHase) based on t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6224be02c9405c5c6b87f2ea3a758d2
Autor:
Eszter Csibra, Tillmann Heinisch, Brett Garabedian, Philippe Marlière, Thomas R. Ward, Sven Panke, Jaicy Vallapurackal, Fabian Schwizer, Vitor B. Pinheiro, Markus Jeschek
Publikováno v:
Chemical Science, 9 (24)
Chemical Science
Chemical Science
Artificial metalloenzymes (ArMs hereafter) combine attractive features of both homogeneous catalysts and enzymes and offer the potential to implement new-to-nature reactions in living organisms. Herein we present an E. coli surface display platform f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62e06eab82ccacf8b7e91c3a9ee6660c
https://edoc.unibas.ch/70533/
https://edoc.unibas.ch/70533/
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
Publikováno v:
Journal of the American Chemical Society, vol 139, iss 48
Copper–hydroperoxido species (Cu II –OOH) have been proposed to be key intermediates in biological and synthetic oxidations. Using biotin–streptavidin (Sav) technology, artificial copper proteins have been developed to stabilize a Cu II –OOH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f7ff6abceaf19cd2d837a565283a3c8
Autor:
Tillmann Heinisch, Tilman Schirmer, Thomas R. Ward, Victor Muñoz Robles, Marc Dürrenberger, Agustí Lledós, Jean-Didier Maréchal
Publikováno v:
Journal of the American Chemical Society. 136:15676-15683
An artificial imine reductase results upon incorporation of a biotinylated Cp*Ir moiety (Cp* = C5Me5(-)) within homotetrameric streptavidin (Sav) (referred to as Cp*Ir(Biot-p-L)Cl] ⊂ Sav). Mutation of S112 reveals a marked effect of the Ir/streptav
Autor:
John A. McIntosh, Tillmann Heinisch, Sabine Brinkmann-Chen, Frances H. Arnold, Sheel C. Dodani, Jackson K. B. Cahn
Publikováno v:
ChemBioChem
A novel cytochrome P450 enzyme TxtE was recently shown to catalyze the direct aromatic nitration of L-tryptophan. This unique chemistry induced us to ask whether TxtE could serve as a platform for engineering new nitration biocatalysts, as a replacem