Structure-function studies of oxidative stress enzymes
At a molecular level, we study the structure-function relationships of a number of proteins that play an important role in oxidative stress and cellular detoxification. To better understand the catalytic mechanisms and the intramolecular electron (and possibly proton) transfer at the origin of the functional properties of these proteins, we aim in particular at determining the structure and environment heme of active sites (NOS, NOS-like proteins, cytochromes P450, oxygen carriers, amyloid β-heme complex), non-heme centers (metal-peptide complexes, superoxide reductase) and flavin (flavoproteins belonging to the pyridine nucleotide-disulfide oxidoreductases family , NOS reductase domain).
A wide range of methodologies is implemented. It includes enzymology, molecular biology, rapid kinetics measurements, biomimetic chemistry, vibrational spectroscopies (IR and Raman), electronic absorption and electron spin resonance (conventional and pulsed EPR, ENDOR), and bioinformatics (molecular dynamics, docking).