A new EPR facility for the Centre for Chemical Biology
Lead Research Organisation:
University of Leicester
Department Name: Chemistry
Abstract
There are a number of experimental methods that people use to obtain answers to specific biological questions. In most cases, however, one single technique cannot provide a complete answer. Because of this, it is common practice to use more than one experimental technique and then to combine all the information together to build up a detailed picture of what is happening. One very useful techinque that is under-utilised in the UK is electron paramagnetic resonance (EPR). This method is capable of detecting free (unpaired) electrons. This is useful because the unpaired electrons act as 'spies' on the molecule and can provide information on local environment. This means that EPR can be used to report on biological (free) radicals, on (paramagnetic) metal centres in biological systems and on protein dynamics. At Leicester, we do not have access to an EPR facility that is suitable for biological work. This slows our work down because it means that we cannot obtain some of the information that we need as fast as we would like to. The current proposal seeks funding to address this problem.
Technical Summary
The aim of this proposal is to establish a new continuous wave EPR facility for the Centre for Chemical Biology at Leicester to support a number of well-funded mechanistic and structural studies on a range of biological systems. This is a multidisciplinary, multi-user bid that includes staff across two faculties, several departments and two institutions. This facility will play an essential part in the long-term development of the Centre by making it possible for us to take advantage of the speed and sensitivity of modern EPR equipment. The technical expertise that we need to suport this new facility is already on-site.
Publications
Millett ES
(2012)
Heme-containing dioxygenases involved in tryptophan oxidation.
in Current opinion in chemical biology
Efimov I
(2011)
Structure and Reaction Mechanism in the Heme Dioxygenases
in Biochemistry
Chauhan N
(2008)
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase.
in Biochemistry
Basran J
(2008)
A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase.
in Biochemistry
Description | We set up a new EPR facility at Leicester |
Exploitation Route | Spectroscopic analyses on metalloproteins (by EPR) |
Sectors | Manufacturing including Industrial Biotechology Pharmaceuticals and Medical Biotechnology |