Peroxiredoxins (Prxs) are ubiquitous thiol peroxidases that are involved in the reduction of peroxides. It has been reported that prokaryotic Prxs generally show greater structural robustness than their eukaryotic counterparts, making them less prone to inactivation by overoxidation. This difference has inspired the search for new antioxidants from prokaryotic sources that can be used as possible therapeutic biodrugs. Bacterioferritin comigratory proteins (Bcps) of the hyperthermophilic archaeon Sulfolobus solfataricus that belong to the Prx family have recently been characterized. One of these proteins, Bcp1, was chosen to determine its antioxidant effects in H9c2 rat cardiomyoblast cells. Bcp1 activity was measured in vitro under physiological temperature and pH conditions that are typical of mammalian cells; the yeast thioredoxin reductase (yTrxR)/thioredoxin (yTrx) reducing system was used to evaluate enzyme activity. A TAT-Bcp1 fusion protein was constructed to allow its internalization and verify the effect of Bcp1 on H9c2 rat cardiomyoblasts subjected to oxidative stress. The results reveal that TAT-Bcp1 is not cytotoxic and inhibits H₂O₂-induced apoptosis in H9c2 cells by reducing the H₂O₂ content inside these cells.

中文翻译：

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在古细菌领域中发现抗氧化分子：来自Sulfolobus solfataricus的Peroxiredoxin Bcp1保护H9c2心肌母细胞免受氧化应激。

过氧化物酶（Prxs）是普遍存在的巯基过氧化物酶，与过氧化物的还原有关。据报道，原核Prxs通常比真核Prxs具有更好的结构坚固性，从而使其不易因过氧化而失活。这种差异激发了人们从原核生物来源寻找新的抗氧化剂的可能性，这些抗氧化剂可以用作治疗性生物药物。最近已鉴定了属于Prx家族的嗜热古细菌Sulfolobus solfataricus的细菌铁蛋白交换蛋白（Bcps）。选择了这些蛋白质之一Bcp1，以确定其在H9c2大鼠心肌细胞中的抗氧化作用。在体外测量Bcp1活性在哺乳动物细胞典型的生理温度和pH条件下; 酵母硫氧还蛋白还原酶（y TrxR）/硫氧还蛋白（y Trx）还原系统用于评估酶活性。TAT-Bcp1融合蛋白被构建以使其内在化，并验证Bcp1对H9c2大鼠心肌成纤维细胞受到氧化应激的影响。结果表明，TAT-BCP1不是细胞毒性并抑制ħ ₂ ö ₂诱导的细胞凋亡的H9c2细胞通过减少为H ₂ ö ₂这些细胞内的内容。