May 2022 - present - Lecturer in Biochemistry - University of East Anglia - School of Biological Sciences

Aug 2015 - Apr 2022 - Post doctoral research associate - School of Biosciences - University of Sheffield

Jan 2012 - Jul 2015 - Post doctoral research assistant - School of Biochemistry - University of Bristol

Oct 2007 - Dec 2011 - PhD candidate - Department of Biochemistry - John Innes Centre

Oct 2004 - Jul 2007 - BSc (Hons) Biochemistry - Schools of Biological Sciences - University of East Anglia

Cryogenic electron microscropy (cryo-EM), protein engineering, protein design, protein purification, spectroscopy, enzymology

My research centres on structural and functional studies of photosynthetic protein complexes to understand the molecular mechanisms that convert light energy into useful chemical forms. Using the knowledge gained from my fundamental studies, I engineer photosynthetic organisms to harvest more of the solar spectrum and to improve the efficiency of downstream processes that store the captured energy as a proton-motive force that is ultimately used to produce ATP for the cell.

My current, ongoing research themes are:

1 – Understanding the structure and function of bacterial light-harvesting complexes

Light-harvesting complexes capture light and transfer the energy to reaction centres where the energy is “trapped” by initiating a series of electron transfers that reduce quinone to quinol. However, the requirement to pack as many light-harvesting pigments around the reaction centre whist simultaneously creating a pathway by which quinones can enter and leave during turnover are conflicting. By determining the structures of reaction centre and light-harvesting complexes from multiple species of purple bacteria using cryo-EM, I am building an understanding of how evolution has balanced these opposing requirements and uncovering strategies that may allow enhanced light harvesting and quinone transport to be engineered into the same system.

2 – Understanding and enhancing quinone turnover in cytochrome bc₁ and b₆f complexes

The rate-limiting step in photosynthesis is quinol oxidation at the cytochrome bc₁ (bacteria), and cytochrome b₆f (plants, algae and cyanobacteria) complexes. The simplest forms of these complexes, found in many species of bacteria, contain only three subunits, which provide the minimal unit required for function. However, evolution has increased the complexity of these complexes through the addition of supernumerary subunits that enhance turnover or add additional functions. Through structure/function studies of photosynthetic cytochrome bc₁ and b₆f complexes I seek to understand the ways in which evolution has overcome rate limitations in these enzymes and use that knowledge to enhance photosynthesis in organisms that lack these adaptations.

3 – Enhancing light harvesting through the absorption of new wavelengths of light

Photosynthetic organisms are brightly coloured because their photosynthetic pigments only absorb a limited amount of the solar spectrum. I aim to increase the spectral range that can be absorbed by photosynthetic organisms to increase the amount of solar energy that is converted into chemical forms. I use protein design and protein engineering to replace the native pigments in light-harvesting complexes with non-native alternatives, or to add entirely new components to the existing light-harvesting antenna network.

4 – Integrating light-harvesting complexes and reaction centres into new electron transport chains and bioelectronics

With collaborators (including at UEA, Sheffield Bristol, Leeds, and the technical university of Munich), I use photosynthetic complexes to drive a variety of electrochemical processes either in photosynthetic organisms, in in vitro systems or in bio-solar cells and biosensors.