Open AccessNRVS and DFT of MitoNEET: Understanding the Special Vibrational Structure of a [2Fe-2S] Cluster with (Cys)3(His)1 Ligation
Author(s) -
Leland B. Gee,
Vladimir Pelmenschikov,
Cécile Mons,
Nakul Mishra,
Hongxin Wang,
Yoshitaka Yoda,
Kenji Tamasaku,
Marie-Pierre Golinelli-Cohen,
Stephen P. Cramer
Publication year - 2021
Publication title -
biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.43
H-Index - 253
eISSN - 1520-4995
pISSN - 0006-2960
DOI - 10.1021/acs.biochem.1c00252
Subject(s) - density functional theory , chemistry , cluster (spacecraft) , function (biology) , protein structure , mitochondrion , oxygen , crystallography , biophysics , biochemistry , computational chemistry , biology , genetics , organic chemistry , computer science , programming language
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 57 Fe nuclear resonance vibrational spectroscopy with density functional theory calculations to understand the novel properties of this important protein.