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Ultra–high‐resolution structure and charge‐density analysis of high‐potential iron–sulfur protein
Author(s) -
Takeda Kazuki,
Miki Kunio
Publication year - 2017
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14036
Subject(s) - metalloprotein , chemistry , cluster (spacecraft) , sulfur , charge density , iron–sulfur cluster , electronic structure , crystallography , high resolution , valence (chemistry) , low resolution , resolution (logic) , valence electron , density functional theory , chemical physics , electron , metal , computational chemistry , physics , biochemistry , enzyme , remote sensing , organic chemistry , quantum mechanics , artificial intelligence , computer science , programming language , geology
The high‐potential iron–sulfur protein (Hi PIP ) is a small (~ 80 residues) soluble metalloprotein functioning as an electron carrier in photosynthetic bacteria. Hi PIP has one Fe 4 S 4 cluster at its molecular center. Its electronic structure is important for understanding electron transport. We recently succeeded in determining an ultra–high‐resolution structure and analyzing the charge‐density of Hi PIP by using X‐ray diffraction data at 0.48 Å resolution. The distribution of valence electrons in the iron–sulfur cluster and in the protein environment were clearly visualized, which is the first successful case for metalloproteins. In addition, a topological analysis of the charge density provided information about the electronic structure of the cluster.