Alkyl hydroperoxide reductase subunit F (AhpF) is a well-known flavoprotein that transfers electrons from pyridine nucleotides to the peroxidase protein AhpC via redox-active disulfide centers to detoxify hydrogen peroxide. However, study of AhpF has historically been limited to particular eubacteria, and the connection between the functional and structural properties of AhpF remains unknown. The present study demonstrates the dual function of Pseudomonas aeruginosa AhpF (PaAhpF) as a reductase and a molecular chaperone. It was observed that the functions of PaAhpF are closely linked with its structural status. The reductase and foldase chaperone function of PaAhpF predominated for its low-molecular-weight (LMW) form, whereas the holdase chaperone function of PaAhpF was found associated with its high-molecular-weight (HMW) complex. Further, the present study also demonstrates the multiple function of PaAhpF in controlling oxidative and heat stresses in P. aeruginosa resistance to oxidative and heat stress.

中文翻译：

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铜绿假单胞菌中烷基氢过氧化物还原酶亚基 F (AhpF) 的功能特性和寡聚状态

烷基氢过氧化物还原酶亚基 F (AhpF) 是一种众所周知的黄素蛋白，它通过氧化还原活性二硫化物中心将电子从吡啶核苷酸转移到过氧化物酶蛋白 AhpC 以解毒过氧化氢。然而，AhpF 的研究历来仅限于特定的真细菌，AhpF 的功能和结构特性之间的联系仍然未知。本研究证明了铜绿假单胞菌 AhpF (PaAhpF) 作为还原酶和分子伴侣的双重功能。据观察，PaAhpF 的功能与其结构状态密切相关。PaAhpF 的还原酶和折叠酶伴侣功能以其低分子量 (LMW) 形式占主导地位，而发现 PaAhpF 的保持酶伴侣功能与其高分子量 (HMW) 复合物有关。更多，