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Using new Fourier transform voltammetry methods to map electron transfer in bio-hydrogen producing enzymes

   Department of Chemistry

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  Dr A Parkin  No more applications being accepted  Funded PhD Project (UK Students Only)

About the Project


The EU target of net zero greenhouse gas emissions by 2050 will only be met by developing new energy technologies, including methods to synthesise fuel molecules as a stable and transportable store of seasonal solar and wind energy. Hydrogen is particularly important as it is compatible with existing natural gas technologies. The outstanding modern scientific advances made in DNA sequencing, molecular biology and protein structure determination have made the development of enzyme-based biofuel technologies a reality, but such applications require a complementary toolkit of physical chemical methods that can dissect how sequence and structure relates to function. As part of the £1.7mill project, “Modernising electrochemical enzymology to map electron transfer” this PhD Studentship will utilise the powerful new electrochemical techniques being developed by the Parkin group to “see” the electron-transfer processes of the highly evolved and essential electron-transfer reaction centres in hydrogen-producing redox-enzymes, and de-convolute their role in electrocatalysis.


Hydrogenases (H2ases) are H2-electrocatalysts built solely of iron- or iron-nickel active sites that operate at comparable speed and efficiency to platinum. The aim of this PhD project is to provide the first ever measurements that plot the rates and energetics of each electron hopping step along a whole H2-enzyme electron transfer relay to map how enzymatic “wiring” controls biological H2-catalysis. The methods will be extended to previously uncharacterised [FeFe]-enzymes via collaboration with anaerobic digestion experts at the University of York, and collaborators in Germany to enable us to dissect the role of H2-metabolism within microbial niches including technologies that convert waste into biofuel.

Experimental Approach

The project will utilise molecular biology methods for carrying out site-directed mutagenesis and protein electrochemistry. To probe how electron transfer influences oxidation state changes at the active site you will collaborate with the group of Prof Neil Hunt whose 2D-IR technique lets us “see” the active site states of H2ases with unparalleled signal sensitivity.


This project will showcase a novel enzyme-electrochemical toolkit to provide completely new insight into the mechanism of biological hydrogen-production, deconvoluting the structure-function relationship and providing a blueprint for using sustainable metals for production of the ultimate low-carbon fuel.


This project will build on the Parkin group’s track record in metalloenzyme mechanistic electrocatalysis and method development as well as Alison’s extensive (from PhD onwards!) expertise in H2ase electrochemistry.1-4 This PhD project will be carried out in close collaboration with a postdoctoral researcher who is developing new computational analysis methods to probe biological electron transfer mechanisms. Training will be provided in all aspects of the work. The Parkin group forms part of the Chemical Biology sub-group of the York Structural Biology Laboratory. We therefore have access to a suite of interdisciplinary chemical, biochemical, microbiology and molecular biology lab spaces, all fully equipped and supported by a phenomenal lab technician. You will be joining a thriving and growing team.

All Chemistry research students have access to our innovative Doctoral Training in Chemistry (iDTC): cohort-based training to support the development of scientific, transferable and employability skills: https://www.york.ac.uk/chemistry/postgraduate/training/idtc/    

The Department of Chemistry holds an Athena SWAN Gold Award and is committed to supporting equality and diversity for all staff and students. The Department strives to provide a working environment which allows all staff and students to contribute fully, to flourish, and to excel: https://www.york.ac.uk/chemistry/ed/

For more information about the project, click on the supervisor's name above to email the supervisor. For more information about the application process or funding, please click on email institution

This PhD will formally start on 1 October 2023. Induction activities may start a few days earlier.

To apply for this project, submit an online PhD in Chemistry application: https://www.york.ac.uk/study/postgraduate/courses/apply?course=DRPCHESCHE3

You should hold or expect to achieve the equivalent of at least a UK upper second class degree in Chemistry or a related subject. Please check the entry requirements for your country: https://www.york.ac.uk/study/international/your-country/

Funding Notes

Studentships are fully funded for 3.5 years by the Department of Chemistry and a European Research Council grant (funded through the UKRI Frontier Research Guarantee) and cover: (i) a tax-free annual stipend (£17,668 2022/23), (ii) tuition fees at the home rate, (iii) funding for consumables.
Selection process:
Following the deadline - 7th January 2023 candidates may be invited to a preliminary interview with the project supervisor. Shortlisted candidates will be invited to a panel interview on a date to be confirmed.
Candidates will be notified of the outcome of the panel’s decision soon after interview.


1. Lloyd-Laney, H. O. et al, Using Purely Sinusoidal Voltammetry for Rapid Inference of Surface-Confined Electrochemical Reaction Parameters. Analytical Chemistry 2021, 93 (4), 2062-2071.
2. Adamson, H. et al, Analysis of HypD Disulfide Redox Chemistry via Optimization of Fourier Transformed ac Voltammetric Data. Analytical Chemistry 2017, 89 (3), 1565-1573.
3. Adamson, H.; Bond, A. M.; Parkin, A., Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry. Chemical Communications 2017, 53 (69), 9519-9533.
4. Adamson, H. et al, Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site. Journal of the American Chemical Society 2017, 139 (31), 10677-10686.

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