The intermolecular amination of C–H bonds is an enabling transformation for the synthesis of nitrogen-containing molecules; however, developing catalysts for this class of reactions is very challenging. Now, an iron-based enzyme for this reaction has been engineered, demonstrating that a protein can confer a difficult new function upon an otherwise unreactive base metal.
Nobel Prize in Chemistry 2018
The 2018 Nobel Prize in Chemistry was awarded to Frances H. Arnold “for the directed evolution of enzymes” and the other half jointly to George P. Smith and Gregory P. Winter “for the phage display of peptides and antibodies”. Together their pioneering work harnesses the processes of evolution for the generation of novel biological compounds. These tools have transformed the production of pharmaceuticals such as monoclonal antibodies and renewable fuels.
This Collection presents research, review, news and comment articles from Nature Research to celebrate the award. The collection content is editorially independent and the sole responsibility of Springer Nature.
Directed evolution optimizes protein function through successive generations of random mutation, artificial selection and screening. This design algorithm provides a reliable approach to engineering proteins with new and useful properties, and helps us to understand how natural evolution occurs.
Discovery of a regioselectivity switch in nitrating P450s guided by molecular dynamics simulations and Markov models
A collaborative approach between experiment and simulation has revealed a single mutation in the F/G loop of the newly described nitrating cytochrome P450 TxtE that controls loop dynamics and, more surprisingly, the regioselectivity of the reaction. This mutation is present in a subset of homologous nitrating P450s that produce a previously unidentified biosynthetic intermediate, 5-nitro-L-tryptophan.
Recent reports on directed evolution broaden the scope of evolutionary enzyme engineering.
A genetically encoded platform can produce chiral organoboranes in bacteria with high turnover, enantioselectivity and chemoselectivity, and can be tuned and configured through DNA manipulation.
The inventor of humanized monoclonal antibodies and cofounder of Cambridge Antibody Technology, Greg Winter, muses on the future of antibody therapeutics and UK life science innovation.