BEGIN:VCALENDAR VERSION:2.0 PRODID:-//jEvents 2.0 for Joomla//EN CALSCALE:GREGORIAN METHOD:PUBLISH BEGIN:VEVENT UID:78ae0246373458f50b97859fbf107853 CATEGORIES:Colloquium CREATED:20201217T164624 SUMMARY:Professor Cathleen Zeymer, Technical University of Munich, Germany DESCRIPTION:
Design and engin eering of lanthanide-binding proteins: from de novo metal coordination to catalysis
The chemical and pharmaceutical industry is under increasing pressure to replace traditional chemical catalysis with sustainable biocatalytic approaches. However, it r emains a major challenge to develop novel enzymes for chemical reactions be yond nature’s synthetic repertoire. A successful strategy is the developmen t of artificial metalloenzymes, which are designed rationally to combine th e catalytic properties of an abiotic metal cofactor with the chiral environ ment of a protein scaffold that provides stereoselectivity. These systems a re genetically encodable and therefore amenable to optimization by directed evolution. This technique mimics natural selection in the laboratory throu gh iterative cycles of mutagenesis and screening. We recently established t he formation of specific metal-protein complexes from highly stable, comput ationally designed protein scaffolds. The metal ions are incorporated by da tive anchoring, which exploits direct coordination by natural amino acids o f the protein. We now work on turning these de novo metalloprotein s into a biocatalytic platform for synthetically valuable reactions, such a s stereoselective carbon-carbon bond formations. Specifically, we developed a de novo TIM barrel scaffold with femtomolar affinity for lantha nides, where metal binding can be observed by sensitizing the element-speci fic luminescence. Lanthanide ions are not only potent Lewis acid catalysts; they also promote photoredox chemistry. Our ongoing work thus focuses on t he development of artificial lanthanide enzymes.
Hosted by Pr ofessor Sagar Khare
For Zoom meeting information, please con
tact Loretta Lupo @
Design and engineering of lanthanide-binding proteins: from de novo metal coordination to catalysis
The chemical and pharmaceutical industry is under increasing pre ssure to replace traditional chemical catalysis with sustainable biocatalyt ic approaches. However, it remains a major challenge to develop novel enzym es for chemical reactions beyond nature’s synthetic repertoire. A successfu l strategy is the development of artificial metalloenzymes, which are desig ned rationally to combine the catalytic properties of an abiotic metal cofa ctor with the chiral environment of a protein scaffold that provides stereo selectivity. These systems are genetically encodable and therefore amenable to optimization by directed evolution. This technique mimics natural selec tion in the laboratory through iterative cycles of mutagenesis and screenin g. We recently established the formation of specific metal-protein complexe s from highly stable, computationally designed protein scaffolds. The metal ions are incorporated by dative anchoring, which exploits direct coordinat ion by natural amino acids of the protein. We now work on turning these de novo metalloproteins into a biocatalytic platform for syntheticall y valuable reactions, such as stereoselective carbon-carbon bond formations . Specifically, we developed a de novo TIM barrel scaffold with fe mtomolar affinity for lanthanides, where metal binding can be observed by s ensitizing the element-specific luminescence. Lanthanide ions are not only potent Lewis acid catalysts; they also promote photoredox chemistry. Our on going work thus focuses on the development of artificial lanthanide enzymes .
Hosted by Professor Sagar Khare
For Zoom mee
ting information, please contact Loretta Lupo @