Chevriau Jonathan, Zerbetto De Palma Gerardo, Alleva Karina, Zeida Ari
Instituto de Química y Fisicoquímica Biológica (IQUIFIB), Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Junín 956, Buenos Aires, Argentina.
Facultad de Farmacia y Bioquímica, Departamento de Fisicomatemática, Universidad de Buenos Aires, Buenos Aires, Argentina.
Biophys Rev. 2025 Feb 20;17(2):301-308. doi: 10.1007/s12551-025-01288-9. eCollection 2025 Apr.
Hydrogen peroxide (HO) is a key reactive oxygen species involved in cellular redox signaling and oxidative stress. Due to its polar nature, its transport across membranes is regulated by aquaporins (AQPs), membrane channels traditionally known for HO transport. Certain AQPs, known as peroxiporins, facilitate selective HO permeation, playing critical roles in mantaining redox homeostasis. This review summarizes insights from molecular dynamics (MD) simulations into the mechanisms of HO transport through AQPs. Key structural regions, such as the selectivity filter (SF) and NPA motif, influence HO permeation, with energy profiles revealing differences from HO transport. While molecular mimicry suggests similarities in the movement of HO and HO, specific interactions and energetic barriers highlight the complexity of the process. We highlight the need for integrating computational and experimental findings for further studies to unify mechanistic understanding and develop applications in redox biology.
过氧化氢（HO）是参与细胞氧化还原信号传导和氧化应激的关键活性氧物种。由于其极性性质，其跨膜运输受水通道蛋白（AQP）调节，AQP是传统上已知的负责HO运输的膜通道。某些被称为过氧化物通道蛋白的AQP促进HO的选择性渗透，在维持氧化还原稳态中发挥关键作用。本综述总结了分子动力学（MD）模拟对HO通过AQP运输机制的见解。关键结构区域，如选择性过滤器（SF）和NPA基序，影响HO的渗透，能量分布揭示了与HO运输的差异。虽然分子模拟表明HO和HO的运动有相似之处，但特定的相互作用和能量障碍突出了该过程的复杂性。我们强调需要整合计算和实验结果，以便进一步研究，以统一机理理解并开发氧化还原生物学中的应用。
