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Dr Ross Anderson

Dr Ross Anderson

Dr Ross Anderson
BSc, PhD(H.-W.)

Senior Lecturer

Area of research

Design and construction of artificial oxidoreductases

Office Room C.101f
Biomedical Sciences Building,
University Walk, Clifton BS8 1TD
(See a map)

+44 (0) 117 331 2151

Summary

The design of new proteins and enzymes remains one of the great challenges in biochemistry and tests our fundamental understanding of both the nature of protein as a material and the principles of enzymatic catalysis. Unlocking the exceptionally diverse and powerful array of chemistries exhibited by natural enzymes promises routes to new drugs, therapies and green industrial processes.

Most approaches to this end have focused on modifying natural enzymes to impart new or altered catalytic function. The problems that often hinder the re-engineering of naturally evolved proteins and enzymes are due to the layers of complexity that nature incorporates through natural selection into a protein’s complex 3D structure.

Simplified manmade protein scaffolds offer a means to avoid such complexity, learn the principles guiding functional protein assembly and render the modular assembly of enzymatic function a tangible reality. This approach is illustrated through the assembly of artificial oxygen binding proteins that reproduce the function of natural proteins such as myoglobin in simple heme-binding 4-helix bundles untouched by natural selection. The tractable design process that we employ resolves the roles of individual amino acids with their function and opens the door to the powerful oxygenic catalysis common to heme-containing enzymes.

In my laboratory, we use this simple protein design approach to construct artificial oxidoreductase enzymes that integrate functional elements common to natural redox enzymes - e.g. electron/proton transfer, ligand/substrate binding and light harvesting - in a discrete manmade protein that is wholly fabricated within a living organism.

Biography

Ross Anderson’s research is focussed on the engineering of de novo designed redox proteins and enzymes, and their subsequent integration into both living organisms and artificial cell-like entities. Ross studied Chemistry at Newcastle University and carried out his PhD in Biomimetic Macrocyclic Chemistry at Heriot-Watt University. He then moved into the field of Biological Inorganic Chemistry with Prof. Stephen Chapman, FRSE, at the University of Edinburgh, studying the natural heme-containing dioxygenases indoleamine and tryptophan 2,3-dioxygenase. From here Ross undertook further postdoctoral research at the University of Pennsylvania in the lab of Prof. Les Dutton, FRS, where he worked on the assembly of simple artificial proteins capable of reproducing sophisticated functional elements common to oxidoreductase enzymes.  

Ross was awarded a Royal Society University Research Fellowship in 2009 to set up his lab in the School of Biochemistry at the University of Bristol. Since then, his lab has explored the in vivo assembly of functional artificial proteins and enzymes funded by the Royal Society and the BBSRC, and in collaboration with Prof. Stephen Mann, FRS (Bristol Chemistry) and Dr. Adam Perriman (Bristol Cell and Molecular Medicine), they are using a combination of protein engineering, de novo protein design and materials chemistry to construct redox cascades in protocellular microdroplets. This collaborative project is funded by the BBSRC through the BrisSynBio (Bristol Synthetic Biology) centre.

  • 2009-present    Royal Society University Research Fellow (URF), School of Biochemistry, University of Bristol 
  • 2006-2009        Postdoctoral Research Associate, Department of Biochemistry and Biophysics, University of Pennsylvania
  • 2003-2006        Postdoctoral Research Associate, School of Chemistry, University of Edinburgh
  • 1999-2003        PhD, Heriot-Watt University
  • 1996-1999        BSc, Chemistry, Newcastle University

Teaching

I currently teach on the following courses:

  • 1st year Biological Chemistry 1A - nucleotides and cofactors lectures, calculations workshop
  • 1st year Biological Chemistry 1B - metals in biology and quantum tunneling lectures
  • 2nd year Organisation and Communication in Cells - redox reactions in billogy lectures and enzyme kinetics labs 
  • 3rd year Synthetic Biology Options Course - enzyme design and synthetic biology ethics
  • 4th Year MSci - Synthetic Biology Options Course - computational protein design & directed evolution lectures, labs & workshops
  • MSc in Biophysics lectures - enzyme kinetics and metalloprotein biophysics
  • Synthetic Biology CDT (PhD) - computational and de novo enzyme design

I am also the Year in Industry Coordinator for the School of Biochemistry

Memberships

Organisations

School of Biochemistry

Other sites

School of Biochemistry staff

Recent publications

View complete publications list in the University of Bristol publications system

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