NRVS and DFT of MitoNEET: Understanding the Special Vibrational Structure of a [2Fe-2S] Cluster with (Cys)₃(His)₁ Ligation

The human mitochondrial protein, mitoNEET (mNT), belongs to the family of small [2Fe-2S] NEET proteins that bind their iron–sulfur clusters with a novel and characteristic 3Cys:1His coordination motif. mNT has been implicated in the regulation of lipid and glucose metabolisms, iron/reactive oxygen species homeostasis, cancer, and possibly Parkinson’s disease. The geometric structure of mNT as a function of redox state and pH is critical for its function. In this study, we combine 57Fe nuclear resonance vibrational spectroscopy with density functional theory calculations to understand the novel properties of this important protein.人类线粒体蛋白mitoNEET（mNT）隶属于小型[2Fe-2S]类NEET蛋白家族，该家族蛋白以新颖且特征性的3Cys:1His配位基序结合其铁硫簇。mNT已被证实参与脂质与葡萄糖代谢、铁/活性氧稳态及癌症的调控，且可能与帕金森病相关。mNT的几何结构随氧化还原状态与pH的变化对其功能至关重要。本研究将57Fe核共振振动光谱法（57Fe nuclear resonance vibrational spectroscopy）与密度泛函理论（density functional theory）计算相结合，以阐明该重要蛋白的新颖特性。