90 citations · 182 across the 14 of their papers we have counts for
14 papers
Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction
Virgile Adam, Antoine Royant, Vincent Nivière +2
Some sulfate-reducing and microaerophilic bacteria rely on the enzyme superoxide reductase (SOR) to eliminate the toxic superoxide anion radical (O2*-). SOR catalyses the one-elect…
Identification of iron(III) peroxo species in the active site of the superoxide reductase SOR from Desulfoarculus baarsii
Christelle Mathé, Tony A Mattioli, Olivier Horner +4
The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. It specifically reduces superoxide to produce H2O2. Here…
A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor
Julien Valton, Laurent Filisetti, Marc Fontecave +1
The two-component flavin-dependent monooxygenases belong to an emerging class of enzymes involved in oxidation reactions in a number of metabolic and biosynthetic pathways in micro…
The flavin reductase ActVB from Streptomyces coelicolor: characterization of the electron transferase activity of the flavoprotein form
Laurent Filisetti, Julien Valton, Marc Fontecave +1
The flavin reductase ActVB is involved in the last step of actinorhodin biosynthesis in Streptomyces coelicolor. Although ActVB can be isolated with some FMN bound, this form was n…
Superoxide reductase from Desulfoarculus baarsii: reaction mechanism and role of glutamate 47 and lysine 48 in catalysis
M. Lombard, C. Houée-Levin, D. Touati +2
Superoxide reductase (SOR) is a small metalloenzyme that catalyzes reduction of O(2)(*)(-) to H(2)O(2) and thus provides an antioxidant mechanism against superoxide radicals. Its a…
The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotides
V. Nivière, F. Fieschi, J. L. Dećout +1
The NAD(P)H:flavin oxidoreductase from Escherichia coli, named Fre, is a monomer of 26.2 kDa that catalyzes the reduction of free flavins using NADPH or NADH as electron donor. The…