Murielle Lombard

TL;DR: In this article, the authors showed that desulfoferrodoxin behaves as a superoxide reductase enzyme and thus provides new insights into the biological mechanisms designed for protection from oxidative stresses.

TL;DR: UV-visible and electron paramagnetic resonance spectroscopy studies revealed that the ferrous center of desulfoferrodoxin could specifically and efficiently reduce O⨪2, with a rate constant of 6–7 × 108 m −1 s−1, and it was shown that membrane and cytoplasmic E. coli protein extracts, using NADH and NADPH as electron donors, could reduce the O⩪2oxidized form of des sulfuroferrod toxin.

TL;DR: A gene in T. pallidum is described with sequence homologies to a new class of antioxidant systems, named superoxide reductases, recently isolated from sulfate-reducing bacteria, and the question of the importance of superoxide reductionases in mechanisms for detoxifying superoxide radicals is raised.

TL;DR: It is proposed that BH may be involved in the second protonation process corresponding to the release of H2O2 from the iron(III)-hydroperoxo species, and investigated the acido-basic and pH dependence of the redox properties of the active site of SOR from Desulfoarculus baarsii.

TL;DR: The reconstituted spectra for the two intermediates are consistent with formation of transient iron‐peroxide species and are 10 times higher than the corresponding one previously reported in the case of SOR from Desulfoarculus baarsii.