The Project

A defining characteristic of life is the requirement of energy from an external source; we eat, plants absorb light. To maximize the energy gained from the food that we and all oxygen-breathing organisms consume, oxygen is converted to water as a final step and carbon dioxide is released. The oxygen in this equation arises from plants as they convert water, carbon dioxide and light, into oxygen and fuel. This cycle is not merely an auspicious result of billions of years of evolution. The molecular events that allow the processes of respiration and photosynthesis to happen are connected in deep ways, down to shared structures, molecules, and mechanisms.

Natural modular oxidoreductases support electron transfer over long distances and catalysis

At their most basic, respiration and photosynthesis are Nature’s way to capture and convert energy from one form to another. To do this, Nature has evolved complex structures, termed oxidoreductases, that bind molecules that aid in this conversion. These molecules can both absorb light, imparting plants with their colours, and take and give electrons. The oxidoreductases have evolved to take energy from external sources and convert it into forms that can be used by living organisms to grow and survive. The evident complexity of this process belies a central feature of the oxidoreductases involved: evolution has yielded structures that are built from repeats of relatively simple modules. All of respiration and photosynthesis are built on these repeating modules. But despite nearly a century of investigation, where we have outlined how respiration and photosynthesis work in fine detail, we remain unable to construct our own models of these processes. This naturally leads to a question of whether we really understand how these processes occur.

Here we have assembled a team of researchers from multiple academic institutions and disciplines to address deficiencies in our knowledge, with the unified target of building completely new oxidoreductases from scratch. Through this work we will fill holes in our understanding of how Nature captures and converts energy.

Our work begins by combining powerful computational techniques that allow us to design and construct oxidoreductases with tailor made functions. Within a virtual reality framework that we are developing for this project, we will work together in a shared digital space to construct molecular binding sites, alter how molecules take and give electrons or catalyse reactions, and create oxidoreductase modules that, taking inspiration from Nature, we will join to produce more complex functions. With these designs, we will use an iterative ‘build-test-learn’ approach to construct new oxidoreductases that match the activities and actions of those Nature uses in respiration and photosynthesis. By pulling together our expertise in computational biophysical methods, oxidoreductase engineering, modular structure creation, molecular binding site assembly and their chemistry, and the analysis of very fast oxidoreductase functions, our team stands to make a substantial leap in our understanding of how to construct new oxidoreductases that has, so far, remained beyond our grasp.

The principles we establish through this work will help us to better understand the oxidoreductases of respiration and photosynthesis, finally clarifying architectural features that are essential for their assembly and function that have remained opaque for over a century. With our new sets of design principles, we will be able to create oxidoreductases that fulfil our needs in bioscience and biotechnology, from the creation of single structures that produce fuels from light, water and carbon dioxide akin to photosynthesis to biosensors that detect toxins in the environment or signs of disease.

The Team

University of Bristol

J. L. Ross Anderson
Project Lead, and PI
Paulina Dubiel (PDRA With JLRA)
Adrian J. Mulholland
Protein Dynamics Lead, and Co-I
Paul Curnow
Membrane Protein Design Lead, and Co-I
Ben Hardy (PDRA With PC)
Thomas A. A. Oliver
Multi-dimensional Spectroscopy Lead, and Co-I
Fabio Parmeggiani
Computational Design Lead, and Co-I
Sofia Oliveira
Computational Protein Analysis, and Res-Co-I

University of Portsmouth

Bruce R. Lichtenstein
Protein Chemistry and Design Lead, and Co-I
Jessica Berrones-Reyes (PDRA With BRL)

University of East Anglia

Julea Butt
Electron Transport Lead, and Co-I

University College London/Birkbeck

Amadine Marechal
PCET Lead, and Co-I

Position Available:
Research Associate in Ultrafast Dynamics of Photoactive Proteins

The Role

A research associate position in experimental ultrafast dynamics studies of photoactive proteins is available in the School of Chemistry at the University of Bristol, supported by BBSRC Grant BB/W003449/1, Creating and comprehending the circuitry of life: precise biomolecular design of multi-centre redox enzymes for a synthetic metabolism.

The multidisciplinary project aims to design, synthesise and characterise (using novel ultrafast spectroscopies) modular de novo proteins capable of broadband solar energy capture to drive redox catalysis. This approach will provide an unprecedented framework to better understand and exploit the exceptional properties of natural energy and electron conducting proteins.

The research associate will work on the following objectives: (i) contribute to the assembly and characterisation of spectrometers using a new commercial ultrafast laser system to probe photoinduced dynamics spanning 100 femtoseconds to 1 millisecond; (ii) determine the rates of photoinduced electron transfer in designer proteins; (iii) elucidate the ultrafast electronic energy transfer pathways in specially tailored photoactive proteins using 2D electronic spectroscopy.

More information on Tom Oliver’s group can be found at:

Please apply here.

What will you be doing?

You will undertake ultrafast laser laboratory-based studies in the School of Chemistry at the University of Bristol- one of the top ranked Chemistry departments in the UK (1st in REF2021). You will collaborate closely with the multidisciplinary consortium of chemists, biochemists and computational chemists. You will contribute to the construction of transient absorption and transient infrared experiments using a commercial dual-amplified ultrafast laser system and optical parametric amplifiers to probe dynamics between 100 fs and 1 ms.  You will also use an established 2D electronic spectroscopy experiment to monitor ultrafast energy transfer. The rate constants determined from ultrafast studies for energy and electron transfer will be used to identify bottlenecks or potential deficiencies in the synthetic proteins and provide critical feedback in the iterative protein design process. Other techniques will include: 2D electronic-vibrational spectroscopy and time-resolved fluorescence spectroscopy.

You should apply if
The position would suit a talented and motivated early career researcher with a PhD in Physical Chemistry or Physics and experience with ultrafast laser spectroscopy. The following skills and experience are advantageous for the role: use of ultrafast laser amplifiers and optical parametric amplifiers; knowledge of non-linear optics; development of Labview control software; experience with analysis of time-resolved spectra; handling of liquid samples; ability to communicate complex information clearly and accurately in English, both in written and oral forms; ability to work independently and as part of a team.

Additional information
Informal queries should be made to Dr Tom Oliver ( in the first instance.

Funding Provided By: