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:1His coordination motif. mNT has been implicated in the regulation of lipid and glucose metabolisms, iron/reactive oxygen s...

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Published in:Biochemistry (Easton) 2021-08, Vol.60 (31), p.2419-2424
Main Authors: Gee, Leland B, Pelmenschikov, Vladimir, Mons, Cécile, Mishra, Nakul, Wang, Hongxin, Yoda, Yoshitaka, Tamasaku, Kenji, Golinelli-Cohen, Marie-Pierre, Cramer, Stephen P
Format: Article
Language:English
Subjects:
Biochemistry, Molecular Biology
Cysteine - chemistry
Density Functional Theory
Humans
Hydrogen-Ion Concentration
Iron - chemistry
Life Sciences
Lysine - chemistry
Magnetic Resonance Spectroscopy
Mitochondrial Proteins - chemistry
Models, Molecular
Protein Binding
Protein Domains
Structural Biology
Sulfur - chemistry
Vibration
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/acs.biochem.1c00252