NRVS and DFT of MitoNEET: Understanding the Special Vibrational Structure of a [2Fe-2S] Cluster with (Cys)3(His)1 Ligation.
Leland B GeeVladimir PelmenschikovCécile MonsNakul MishraHongxin WangYoshitaka YodaKenji TamasakuMarie-Pierre Golinelli-CohenStephen P CramerPublished in: Biochemistry (2021)
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.
Keyphrases
- density functional theory
- molecular dynamics
- reactive oxygen species
- endothelial cells
- protein protein
- metal organic framework
- papillary thyroid
- oxidative stress
- binding protein
- high resolution
- aqueous solution
- energy transfer
- single molecule
- squamous cell
- induced pluripotent stem cells
- blood glucose
- squamous cell carcinoma
- visible light
- blood pressure
- pluripotent stem cells
- lymph node metastasis
- insulin resistance
- solid state