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Investigating metalloprotein mechanism using ‘physiological’ X-ray absorption spectroscopy

  • Full or part time
  • Application Deadline
    Tuesday, February 04, 2020
  • Funded PhD Project (Students Worldwide)
    Funded PhD Project (Students Worldwide)

Project Description

A wide variety of metalloproteins, utilising a range of earth-abundant metals, are vital to many biological processes. Changes in metal-based oxidation state are critical to the function of metalloproteins with diverse roles in electron transfer and redox catalysis. Structural and coordination changes around metal centres are intimately associated with these redox transitions, and so methods that allow characterisation of the full range of functionally-relevant oxidation states are crucial for an understanding of how metalloproteins work so efficiently.

X-ray absorption spectroscopy (XAS) is an element-sensitive technique that provides information about local geometry and electronic structure. Biological XAS of metalloenzymes can provide information about small changes in local structure that are otherwise hard to determine from crystallographic studies alone, and is a highly complementary technique for structural biology. At present the majority of biological XAS is carried out at cryogenic temperatures, due to problems associated with sample damage by the intense X-ray beams needed for these measurements. In order to gain a better understanding of how metalloproteins work, however, we need to develop methods that allow study under more ‘physiological’ conditions.

This project explores new approaches to X-ray absorption spectroscopy of metalloproteins, coupled with electrochemical control over oxidation state. The project complements chemical biology research within both the School of Chemistry and the Leicester Institute of Structural and Chemical Biology, and involves collaboration with researchers at Diamond Light Source, UK. The successful candidate will gain extensive interdisciplinary training, including significant experience of research at UK-wide large-scale facilities.

Entry requirements

UK Bachelor Degree with at least 2:1 in a relevant subject or overseas equivalent.

University of Leicester English language requirements apply (where applicable) https://le.ac.uk/study/research-degrees/entry-reqs/eng-lang-reqs/ielts-60

Eligibility

UK/EU/International

* International applicants must be able to fund the difference between the UK/EU and the International fees for the duration of their studies.

How to Apply

Please refer to the ’How to Apply’ section at: https://le.ac.uk/study/research-degrees/funded-opportunities/chem-ash-2020

Funding Notes

Fully funded 3.5 years

International students to fund the difference between Home/EU fee

References

1. Introduction to XAFS: a practical guide to x-ray absorption fine structure spectroscopy. G. Bunker, 2010, Cambridge University Press.

2. Spectroscopic analysis of immobilised redox enzymes under direct electrochemical control. P.A. Ash, K.A. Vincent, Chem. Commun. 2012, 48, 1400-1409.

3. Unifying activity, structure and spectroscopy of [NiFe] hydrogenases: combining techniques to clarify mechanistic understanding. P.A. Ash, S.E.T. Kendall-Price, K.A. Vincent, Accounts of Chemical Research 2019, in press.

4. Proton transfer in the catalytic cycle of NiFe hydrogenases: insight from vibrational spectroscopy. P.A. Ash, R. Hidalgo, K.A. Vincent, ACS Catalysis 2017, 7, 2471-2485.

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