the resonance Raman modes of the oxidized and two-electron reduced forms of Npx are related to very tight flavin-protein interactions maintaining a nearly planar conformation of the isoalloxazine tricycle, a low level of H-bonding at the N1/N5 and O2/O4 sites, and a strong H-bond at N3H. They indicate minimal changes in FAD structure and environment upon either NAD(H) binding or reduction of the sulfinic redox center
Cu2+-ion-modified graphene oxide nanoparticles catalyze the H2O2 oxidation of NADH to the biologically active NAD+ cofactor. The catalytic NAD+ cofactor regeneration system may be coupled to NAD+-dependent enzymes
La Carbona, S.; Sauvageot, N.; Giard, J.C.; Benachour, A.; Posteraro, B.; Auffray, Y.; Sanguinetti, M.; Hartke, A.
Comparative study of the physiological roles of three peroxidases (NADH peroxidase, alkyl hydroperoxide reductase and thiol peroxidase) in oxidative stress response, survival inside macrophages and virulence of Enterococcus faecalis