ABSTRACT Plants need light energy to drive photosynthesis, but excess energy leads to the production of harmful reactive oxygen species (ROS), resulting in oxidative inactivation of target enzymes, including the photosynthetic CO2-fixing enzyme, ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). It has been demonstrated in vitro that oxidatively inactivated Rubisco can be reactivated by the addition of reducing agents. Busch et al. (in The Plant Journal, doi: 10.1111/tpj.14617, 2020) recently demonstrated that bundle-sheath defective 2 (BSD2), a stroma-targeted protein formerly known as a late-assembly chaperone for Rubisco biosynthesis, can be responsible for such reactivation in vivo. Here, we propose a working model of the novel redox regulation in Rubisco activity. Redox of Rubisco may be a new target for improving photosynthesis.

中文翻译：

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拟南芥 BSD2 揭示了体内 Rubisco 生理学的新型氧化还原调节

摘要 植物需要光能来驱动光合作用，但过量的能量会导致有害活性氧 (ROS) 的产生，导致目标酶氧化失活，包括光合 CO2 固定酶、核酮糖 1,5-二磷酸羧化酶/加氧酶（鲁比斯科）。体外已经证明，氧化失活的 Rubisco 可以通过添加还原剂重新活化。布施等人。（在 The Plant Journal, doi: 10.1111/tpj.14617, 2020）最近证明束鞘缺陷 2 (BSD2)，一种基质靶向蛋白质，以前称为 Rubisco 生物合成的后期组装伴侣，可以负责这种体内再活化。在这里，我们提出了 Rubisco 活动中新型氧化还原调节的工作模型。Rubisco 的氧化还原可能是改善光合作用的新目标。