The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins

Continuous versus Cyclic Progesterone Exposure Differentially Regulates Hippocampal Gene Expression and Functional Profiles

“…Since mitochondria are a major site of generation of and target for hydrogen peroxide, the mitochondrial Prxs, including Prx3 and Prx5, play an important role in regulation of mitochondrial redox homoeostasis [27]. Prx5 in particular may present broader activity than other antioxidant mitochondrial enzymes [28], [29]. Overexpression of Prx5 has a positive impact on neuronal survival and extension of lifespan; Prx5 deficiency produces signs of oxidative stress, apoptosis, and shortened lifespan [26], [27].…”

Insights into the Alkyl Peroxide Reduction Pathway of Xanthomonas campestris Bacterioferritin Comigratory Protein from the Trapped Intermediate–Ligand Complex Structures

“…The two oxygen atoms of the formate ion can mimic the two oxygen atoms of a peroxide substrate, as has been suggested for the oxygen atoms of acetate and benzoate ligands present in other reported Prx structures. 23,24 It is clear that a long alkyl chain can be attached to the formate carbon within the substrate entrance channel without any hindrance (indicated by an orange dotted arrow in Fig. 4a).…”

“…[1][2][3]10 The tertiary structures of several 1-Cys 11,12 and typical 2-Cys Prxs [13][14][15][16][17][18][19][20] have been determined, and the oligomerization states of typical 2-Cys Prxs were found to be correlated with their activity. 21,22 However, atypical 2-Cys Prxs, [23][24][25][26][27] including the bacterioferritin comigratory protein (BCP), are less well characterized, although some of their biological activities have been illustrated. [28][29][30][31] Here, we report the crystal structure of XcBCP, which is a novel member of the atypical 2-Cys Prxs from the plant pathogen Xanthomonas campestris, in three different states.…”

Cloning, genomic structure, and expression analysis of peroxiredoxin V from bay scallop Argopecten irradians

“…PrxV from A. irradians is emphasized by star. The species and the GenBank accession numbers are given in Table 2. intramolecular disulfide bond when reaction between the peroxidatic cysteine and the resolving cysteine occurs [19,20,26]. While residues around Cys75 and the catalytic site appear to be well conserved, amino acids around Cys177 have less identity.…”