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‘Heme proteins, ubiquitous and essential for every organism’
12 June 2009
Leicester, University of
Research at the chemistry-biology interface has been a major strength in Leicester for many years. Scientists at the Henry Wellcome Building for Biomedical Research have been bringing together equipment, staff and ideas in an attempt to establish a multidisciplinary approach to better study the structure, kinetics and function of biological systems.
On Wednesday 17th June, Dr Pipirou will present the key findings of her Ph.D. research in which she studied the function and mechanism of formation of covalent links inside heme proteins. Carried out in Professor Emma Raven’s lab, Dr Pipirou’s research involved using techniques at the interface between the traditional chemistry and biology disciplines to engineer covalent links, physiologically seen in mammalian proteins, into members of their plant counterparts.
Dr Pipirou’s doctoral research has given valuable insight into the similarities and differences between plant and mammalian heme proteins and has shown that plant proteins can be used as model systems to study the characteristics and function of complex mammalian systems. Dr Pipirou was recently presented with the Royal Society of Chemistry’s 2008 Laurie Vergnano Award, in recognition of her research in this field.
Dr Pipirou commented: ‘Heme, is an iron-containing molecule that is an integral component of many proteins, so-called hemoproteins, in bacteria, plants and animals. It is the component of hemoglobin that gives blood its red color. Heme proteins display a wide range of biological functions; for example, hemoglobin and myoglobin are able to maintain a balanced supply of oxygen by functioning as oxygen transport and binding proteins.’
‘Although the heme is non-covalently bound to many of these proteins, it is now becoming clear that a large number of other proteins use modified versions of heme in which the heme is covalently linked to the protein. The most striking example of such a protein is myeloperoxidase, a member of the mammalian peroxidases, which bears three heme-protein covalent bonds. My Phd work was based on examining how these links are made across different families of heme proteins.’
She said: ‘I will present the type of heme-protein links that we can engineer into plant peroxidases and demonstrate how plant proteins can use the same chemistry and mechanisms that we see for mammalian enzymes. Most importantly, I will discuss what nature has to gain by supporting formation of such heme-protein links or even by “switching them off”.’
Dr Pipirou was recently presented with the Royal Society of Chemistry’s 2008 Laurie Vergnano Award, in recognition of her research in this field.