posted on 2021-07-26, 19:15authored byLeland
B. Gee, Vladimir Pelmenschikov, Cécile Mons, Nakul Mishra, Hongxin Wang, Yoshitaka Yoda, Kenji Tamasaku, Marie-Pierre Golinelli-Cohen, Stephen P. Cramer
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.