Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus

• Published in: Biochimica et biophysica acta. General subjects Vol. 1862; no. 12; pp. 2797 - 2805
• Main Authors: Liu, Wenxia, Liu, Aijun, Gao, Hailong, Wang, Quan, Wang, Limin, Warkentin, Eberhard, Rao, Zihe, Michel, Hartmut, Peng, Guohong
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2018
• Subjects: 1-Cys peroxiredoxins; active sites; AhpC2; Aquifex; Archaea; C-terminal region; Catalysis; Catalytic Domain; crystal structure; cysteine; disulfide bonds; Disulfides - chemistry; electron microscopy; Eubacterium - chemistry; eukaryotic cells; genome; hydrogen peroxide; hydroperoxides; mutagenesis; Oligomerization; Oxidation-Reduction; Peroxidase; peroxiredoxin; Peroxiredoxins - chemistry; Peroxiredoxins - genetics; Peroxiredoxins - isolation & purification; Polymerization; Protein Conformation; reaction mechanisms; signal transduction; Solutions; Sulfonic acid form; sulfonic acids; thiols; topology; Oligomerization; C-terminal region; AhpC; Peroxidase; Prxs; AhpC2; Sulfonic acid form; 1-Cys peroxiredoxins; CP; Tpx; Bcp

Peroxiredoxins (Prxs) are thiol peroxidases that scavenge various peroxide substrates such as hydrogen peroxide (H2O2), alkyl hydroperoxides and peroxinitrite. They also function as chaperones and are involved in signal transduction by H2O2 in eukaryotic cells. The genome of Aquifex aeolicus, a micr...