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Ergebnisse nach Hochschule und Institut
Publikation An artificial metalloenzyme for carbene transfer based on a biotinylated dirhodium anchored within streptavidin(Royal Society of Chemistry, 04/2018) Zhao, Jingming; Bachmann, Daniel G.; Lenz, Markus; Gillingham, Dennis G.; Ward, Thomas R.We report on artificial metalloenzymes that incorporate a biotinylated dirhodium core embedded within engineered streptavidin (Sav hereafter) variants. The resulting biohybrid catalyzes the carbene insertion in C–H bonds and olefins. Chemical- and genetic optimization allows to modulate the catalytic activity of the artificial metalloenzymes that are shown to be active in the periplasm of E. coli (up to 20 turnovers).01A - Beitrag in wissenschaftlicher ZeitschriftPublikation Ferritin encapsulation of artificial metalloenzymes: engineering a tertiary coordination sphere for an artificial transfer hydrogenase(Royal Society of Chemistry, 07/2018) Hestericová, Martina; Heinisch, Tillmann; Lenz, Markus; Ward, Thomas R.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 the streptavidin-biotin technology. The third coordination sphere, provided by ferritin, significantly influences the catalytic activity of an ATHase for the reduction of cyclic imines.01A - Beitrag in wissenschaftlicher ZeitschriftPublikation Immobilization of an artificial imine reductase within silica nanoparticles improves its performance(Royal Society of Chemistry, 2016) Hestericová, Martina; Correro, Maria Rita; Lenz, Markus; Corvini, Philippe; Shahgaldian, Patrick; Ward, Thomas R.Silica nanoparticles equipped with an artificial imine reductase (biotinylated iridium complex conjugated with streptavidin) display marked redn. activity toward cyclic imines and NAD. The method, based on immobilization and protection of streptavidin on silica nanoparticles, shields the biotinylated metal cofactor against deactivation yielding >46,000 turnovers in pure samples and 4000 turnovers in crude cellular exts.01A - Beitrag in wissenschaftlicher Zeitschrift