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Dr Ross Anderson

Dr Ross Anderson

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

Associate Professor in Biological Chemistry

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


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.


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 extensively explored the in vivo assembly of functional artificial proteins and enzymes funded by the Royal Society and the BBSRC. He collaborates with: Prof Adrian Mulholland (Bristol Chemistry) on the computational design and analysis of de novo proteins; Prof Stephen Mann, FRS (Bristol, Chemistry), Prof Adam Perriman (Bristol, CMM) and Dr Nicolas Martin (CNRS, Bordeaux) on the design of artificial protocells; Prof Paddy Royal (Bristol, Physics) and Dr John Russo (Bristol, Maths) on critical soft matter and the construction of multiprotein gels; Dr Chris Pudney (Bath, Chemistry) on catalysis in de novo proteins.

  • 2019-               Associate Professor in Biological Chemistry, University of Bristol
  • 2017-2019        Senior Lecturer, University of Bristol
  • 2009-2017        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


Biological Chemistry 1A/1B - the chemistry of nucleotides and cofactors, metals in biology, quantum tunneling in biology

Macromolecular Structure, Dynamics and Function - cellular redox homeostasis, oxidative stress and non-respiratory use of oxygen & enzyme kinetics labs.

Advanced Options in Biochemistry – computational and iterative de novo enzyme design, ethics in synthetic biology

MSci Synthetic Biology Options - directed evolution, computational protein and enzyme design, high throughput selection and analysis

MSc Biophysics and Molecular Life Sciences - enzymology and metalloprotein chemistry and biophysics

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



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