WebbRubrerythrins (RBRs) are non-heme di-iron proteins belonging to the ferritin-like superfamily. They are involved in oxidative stress defense as peroxide scavengers in a … Rubrerythrin (RBR) is a non-heme iron-containing metalloprotein involved in oxidative stress tolerance within anaerobic bacteria. It contains a di-iron active site, where peroxide is reduced into two water molecules, and a mono-iron rubredoxin-like domain thought to be involved in electron transfer. A majority of … Visa mer As a member of the Ferritin-like superfamily, RBRs primary function is iron storage and detoxification. Rubrerythrins utilize their di-iron centers to bind with reactive oxygen species such as Hydrogen Peroxide, … Visa mer Many formations of RBRs can be identified by four helical structures, chains alpha and beta containing 3 iron atoms. Both N and C-terminals of common RBRs are very similar to Rubredoxin containing amino acid residue sequences. Furthermore, both metalloproteins … Visa mer In a reduced state without exposure to reactive oxygen byproducts, Rubrerythrin contains two water molecules near its di-iron center. During and after exposure to peroxide, Rubrerythrin becomes oxidized, changing rotational conformations beginning around the … Visa mer

Molecules Free Full-Text Disproportionation of H2O2 Mediated …

WebbHeme iron and nonheme dimanganese catalases protect biological systems against oxidative damage caused by hydrogen peroxide. Rubrerythrins are ferritine-like nonheme diiron proteins, which are structurally and mechanistically distinct from the heme-type catalase but similar to a dimanganese KatB enzyme. In order to gain more insight into … Webb18 nov. 2016 · Rubrerythrins (RBRs) are non-heme di-iron proteins belonging to the ferritin-like superfamily. They are involved in oxidative stress defense as peroxide scavengers in … bookshelf background image

Responses of Clostridia to oxygen: from detoxification to adaptive ...

WebbBased on the crystal structures, three possible sequence determinants have been suggested as the cause of a 285 mV increase in reduction potential of the rubredoxin domain of rubrerythrin over rubredoxin by modulating the polar environment around the redox site. Here, electrostatic calculations of crystal structures of rubredoxin and … Webb19 aug. 2011 · Like rubrerythrins, symerythrin contains a π-helical segment in helix C (πC) adjacent to the metallocenter. In addition, as predicted, 6 a π-helical segment (πA) is present in helix A of symerythrin (Fig. 2b). Each of these two π-helices has a Pro at its C-terminal end (Fig 2a) and is associated with a ~20° kink in its core helix. Webboptimale Temperatur (60--75~C, j e naeh Verbindung) und optimaler pH-Wert (6 N HC1). Die Potentialkurve ist der mV-Aehse am _~quivalenzpunkt fast parallel, das _~quivalenzpotentialE~K E liegt bei allen Verbindungenzwisehen 60 und 90 mV. Als Elektrodensystem dient eine gl~nzende Platinelektrode und eine ges~tt. … harvey games