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ROSS Anderson, University of Bristol, United-Kingdom

Totally wired: Amping up the design of de novo bioenergetic components


J. L. Ross Anderson is Professor of Biological Chemistry in the School of Biochemistry at the University of Bristol. After completing his undergraduate and postgraduate studies at the University of Newcastle and Heriot-Watt University respectively, Ross pursued postdoctoral research at the University of Edinburgh with Professor Steve Chapman, FRSE, in bioinorganic enzymology (2003-2006) and then at the University of Pennsylvania with Professor Les Dutton, FRS, where he worked on the de novo design of oxygen-binding heme proteins (2006-2009). From there, he moved to the School of Biochemistry at the University of Bristol with a Royal Society University Research Fellowship to establish his own independent career.

His research group focusses on the de novo design of biocompatible proteins that integrate functional elements common to natural redox enzymes, electron-conducting proteins and the natural photosynthetic apparatus in robust and evolvable new-to-nature protein scaffolds. This provides a versatile platform for testing our understanding of protein electron transfer, captured energy flow through proteins, and enzymatic catalysis, while providing routes to exploiting their desirable functions on our own terms. Recent research highlights from his group include the assembly of a modular toolkit for de novo redox protein design both in soluble and membrane proteins, the construction of nanoscale protein wires, stereoselective abiological chemistry catalysed by evolvable de novo heme-containing enzymes, and the design of an efficient and promiscuous de novo peroxidase.