| Literature DB >> 34310123 |
Leland B Gee1, Vladimir Pelmenschikov2, Cécile Mons3, Nakul Mishra4, Hongxin Wang5, Yoshitaka Yoda6, Kenji Tamasaku6,7, Marie-Pierre Golinelli-Cohen3, Stephen P Cramer5.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2021 PMID: 34310123 PMCID: PMC8672731 DOI: 10.1021/acs.biochem.1c00252
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162