Research focus
One of the key aims of the Redox Biology Joris Messens Lab is to better understand the mechanisms that tightly control the redox homeostasis of the cell under stress conditions. We are studying the mechanisms behind reactive oxygen species (ROS) scavenging, signalling and regulation. Several oxidoreductase proteins, which successively pass on electrons via complex intra- and intermolecular cascades using thiol-disulfide chemistry, are involved. We specialize in the in vitro reconstitution of these thiol/disulfide electron transfer pathways and the study of the kinetics during electron transfer. The focus is on the recurring thioredoxin motive that catalyses so many diverse reactions, from the reduction of oxidized arsenate reductase up to the formation and/or exchange of disulfide bonds during oxidative protein folding and cysteine protection against oxidative stress. The coming years we want to exploit our biochemical, structural and quantum chemical expertise in thiol/redox-chemistry through the following projects:
‘New redox pathways to fight TB’
Tuberculosis (TB), once referred to as the ‘‘white death’’, is a debilitating human disease caused by Mycobacterium tuberculosis (Mtb). Our main aim is to reveal new redox pathways involved in the oxidative stress defence of the bacterial pathogen Mycobacterium tuberculosis during persistence in human macrophages.
‘Oxidoreductases and their role in oxidative protein folding and cysteine protection’
In the periplasm of E. coli, DsbG and DsbC, two thioredoxin-related proteins, control the global sulfenic acid content of the periplasm and protect single cysteine residues from oxidation. We are studying the single cysteine substrates of DsbG and post-translationally modified DsbG proteins.
‘The interaction proteome of oxidative stress signalling in plants’.
One of the warning messages used by living cells under stress is the production of 'Reactive Oxygen Species (ROS). To understand the complex networks of interactions induced under cellular redox stress, we aim to identify and characterize the proteome of sulfenylated cysteine residues (sulfenome) in Arabidopsis thaliana.
For more details, visit the Brussels Center for Redox Biology website at http://redox.vub.ac.be.
