Funding is available in the Protein Structure & Function Group, School of Biological Sciences, for a PhD programme from October 2017, under supervision of Dr Jonathan Worrall, Dr Mike Hough and Dr Dimitri Svistunenko .

Illuminating the catalytic, structural and mechanistic features of a new class of haem peroxidases to dye for

Dye decolourising peroxidases (DyPs) are the most recent family of haem peroxidase to be discovered. The oxidizing potential of these enzymes is driven by the formation of ferryl intermediates, formed on H2O2 activation, that enable them to oxidize synthetic dye molecules widely used in the textile industry (Fig. 1). Some DyPs have been implicated in biomass deconstruction through the oxidative breakdown of lignocellulose. Thus, DyPs have vast potential for use in biotechnology applications. At present, detailed catalytic and substrate reactivity information is sparse across the four sub-families (A to D) of DyPs and there is a strong need to address this to maximize future commercial applications.

At Essex we have identified an A-type DyP from Streptomyces lividans and have characterised its catalytic cycle and unusual dye decolourisation properties (Fig.1). Further to this, our X-ray structural work (including in-crystal generation of relevant intermediates) and EPR spectroscopy of transiently formed free radicals and high-valence haem states have informed on potential substrate binding sites and electron-transfer pathways (Fig. 2). The overarching aim of this studentship is to extend these experimental approaches across several DyP sub-families incorporating new structural and fast reaction methodologies, such as state of the art synchrotron beamlines and time-resolved X-ray crystallography as well as rapid freeze-quench EPR for kinetics studies, to characterise the high-valence catalytic intermediates and tailor this knowledge to generate designer enzymes for commercial applications.

Figure 1: The proposed catalytic mechanism of a dye decolourising haem peroxidase from Streptomyces lividans. The anthraquinone dye RB19 is decolourised through a disproportionation mechanism.		Figure 2: The X-ray structure of S. lividans DtpA

The successful candidate will work under the supervision of Dr Jonathan Worrall, Dr Mike Hough and Dr Dimitri Svistunenko in the Protein Structure & Function Group in the School of Biological Sciences.

Entry requirements and application procedures

Informal queries may be addressed in the first instance to jworrall@essex.ac.uk or mahough@essex.ac.uk or svist@essex.ac.uk. Applications should be submitted electronically by the 30th June 2017. Please use this FindAPhD page to access the University of Essex application form.

The intended start date for this 3-year, fully-funded PhD studentship is 5th October 2017. This scholarship will be to the value of £12,500 per annum plus UK/EU tuition fees. Applicants should write 500 words explaining why they are interested in this project and submit this with their CV.

Download a flyer with this studentship opportunity (a PDF file).

Finally,

If you have your own funds to undertake a PhD programme, and would like to do that in my lab, you will be in a different, significantly smaller circle of competitors. There are several ways to get your PhD funded, for example, via the Boehringer Ingelheim Fonds. There are also other funders. If you feel interested to perform either of the two offered researches and would like to secure your own funds for that, I would be prepared to help your in drafting an application to such funders.