Ultra-high-resolution structure and charge-density analysis of high-potential iron-sulfur protein.
The high-potential iron-sulfur protein (HiPIP) is a small (~ 80 residues) soluble metalloprotein functioning as an electron carrier in photosynthetic bacteria. HiPIP has one Fe4S4cluster 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 HiPIP 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.
Department of Chemistry, Graduate School of Science, Kyoto University, Japan.
Kazuki
K
Takeda
Department of Chemistry, Graduate School of Science, Kyoto University, Japan.
Kunio
K
Miki
D001419:Bacteria / Q000737:chemistry* / Q000145:classification / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D018360:Crystallography, X-Ray; D004579:Electron Transport; D004583:Electrons; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; C007943:high potential iron-sulfur protein
X-ray crystallography; electron transfer; high-potential iron-sulfur protein; photosynthesis; valence electron distribution