Pascale Delangle & Sarah Hostachy

The superoxide radical anion O₂^{• -} is continuously produced by living organisms as a byproduct of aerobic respiration. If not eliminated, this Reactive Oxygen Species (ROS) can cause severe damage in the cell. To prevent such oxidative stress to occur, aerobic organisms exhibit a family of metalloenzymes that catalyze the dismutation of the superoxide radical anion to hydrogen peroxide and dioxygen, the so-called superoxide dismutases (SODs). These are essential enzymes for living organisms, due to their protective role. Several distinct types of SOD exist, that differ in their sequences and in the metals used to conduct the reaction. The most studied include MnSOD, FeSOD or Cu/ZnSOD. In 1996, a novel SOD containing a mononuclear Ni catalytic site was discovered in Streptomyces bacteria. It was later found present in several pathogenic bacteria, but not in humans, which make it an interesting target for antibiotics.

Understanding the mechanism the NiSOD is thus key to establish new ways to combat oxidative stress or to develop new antibiotics strategies. To do so, the CIBEST team develops biomimetic approaches, relying in particular on (pseudo)peptides, in strong collaboration with DCM (Carole Duboc).





Related publications
Domergue J, Pécaut J, Proux O, Lebrun C, Gateau C, Le Goff A, Maldivi P, Duboc C and Delangle P
Mononuclear Ni(II) complexes with a S3O coordination sphere based on a tripodal cysteine-rich ligand: pH tuning of the superoxide dismutase activity.
Inorganic Chemistry, 2019, 58(19): 12775-12785

Domergue J, Guinard P, Douillard M, Pécaut J, Proux O, Lebrun C, Le Goff A, Maldivi P, Delangle P and Duboc C
A bioinspired Ni^II Superoxide dismutase catalyst designed on an ATCUN-like binding motif.
Inorganic Chemistry, 2021, 60(17): 12772-12780