The Biochemistry and Chemistry Departments at the University of Leicester and the Institut Laue-Langevin (ILL, Grenoble, France), jointly invite applications for a three-year PhD programme entitled ‘The Transient Compound I and II intermediates in peroxidases’.
The project will focus on oxygen activation by heme peroxidases. These enzymes use highly oxidized (ferryl) iron intermediates known as Compound I and Compound II (Figure 1). Nature uses these intermediates for a large number of quite different, and sometimes difficult, biological oxidations, but structural characterisation of these species is diffcult. The shared heme structure in all of these enzymes make it highly likely that these intermediates are a defining feature across the family, but the nature of the ferryl heme is not known. The project intends to address this question using neutron (see for example Blakeley *et al.* Curr. Opin. Struct. Biol. * 2008*, *18,* 593-600) and X-ray crystallographic techniques, together with time-resolved approaches (see for example Gumiero *et al*. J. Biol. Chem. * 2011*, *286*, 1260-1268). The PhD project will be located jointly in Grenoble (France), at the ILL, and at the University of Leicester. The range of skills learned will span from neutron diffraction work (ILL) through to protein crystallography (ILL and Leicester), time-resolved crystallography (Leicester), spectroscopy of heme proteins (Leicester) and protein purification and molecular biology (ILL and Leicester). The successful candidate will be employed for a period of up to three years, with a gross salary of around 2350 €/month, together with other benefits depending on the student’s social status (for more details see: * http://www.ill.eu/science-technology/phd-students/phd-recruitment/phd-work-at-the-ill/ *<http://www.ill.eu/science-technology/phd-students/phd-recruitment/phd-work-at-the-ill/>). The project will be jointly supervised by by Dr Peter Moody ( [email protected]), Dr Matthew Blakeley ([email protected]) and Professor Emma Raven ([email protected]). At Leicester, the successful student can be expected to join a thriving multidisciplinary environment based in the new Henry Wellcome Building for Biomedical Science and the Department of Chemistry, and will be exposed to a range of methodologies at the chemistry/biology interface. The Henry Wellcome building is equipped with state-of-the-art equipment and laboratories, including instrumentation for heme protein expression and purification, protein crystallography, biological spectroscopy and mechanistic work. ILL has the world's most advanced facility for macromolecular neutron crystallography. The Grenoble campus includes the European Synchrotron Radiation Facility (ESRF) and the outstation of EMBL as part the Partnership for Structural Biology (PSB<http://www.psb-grenoble.eu/>), with a specialised deuteration laboratory for biological samples (D-Lab<http://www.ill.eu/sites/deuteration/index.htm> ). Applicants should have or expect to obtain a first class or upper second class degree or equivalent in Biochemistry, Chemistry or a related discipline. Academic knowledge of condensed matter physics will be appreciated but is not essential. *Supervisors*: Dr Peter Moody and Professor Emma Raven, University of Leicester, and Dr Matthew Blakeley, ILL, Grenoble. *Contact information*: Dr Peter Moody ([email protected]; +44 ((0)116 2297097), Matthew Blakeley ([email protected]) and Professor Emma Raven ( [email protected]; +44 ((0)116 2297047).
