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:lHis 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 Fe-57 nuclear resonance vibrational spectroscopy with density functional theory calculations to understand the novel properties of this important protein.

Automated summary

This study investigates the structure and function of the human mitochondrial protein mitoNEET, highlighting its significance in regulating metabolism, homeostasis, and disease development. Fe-57 nuclear resonance vibrational spectroscopy and density functional theory calculations are employed to understand the unique properties of this protein.