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- Title
Tuning the geometries of a de novo blue copper protein by axial interactions.
- Authors
Shiga, Daigo; Hamano, Yusuke; Kamei, Misato; Funahashi, Yasuhiro; Masuda, Hideki; Sakaguchi, Miyuki; Ogura, Takashi; Tanaka, Toshiki
- Abstract
The axial interactions of Cu in type 1 copper proteins control the physical characteristics of the proteins. We tuned the geometries of a de novo designed blue copper protein with a four-helical bundle structure. The designed protein axially bound various ligands, such as chloride, phosphate, sulfate, acetate, azide, and imidazole, to Cu, exhibiting a blue or green color. The UV-vis spectral bands were observed at approximately 600 nm and approximately 450 nm, with the A/ A ratios between 0.14 and 1.58. The stronger axial interaction shifted the geometry of the type 1 copper site from trigonal planar geometry (blue copper) toward a tetrahedral-like geometry (green copper). Resonance Raman spectral analyses showed that the phosphate-bound type had the highest-strength Cu-S bond, similar to that of plastocyanin. The chloride-bound type exhibited features similar to those of stellacyanin and nitrite reductase, and the imidazole-bound type exhibited features similar to those of azurin M121E mutant.
- Subjects
COPPER proteins; PROTEIN structure; LIGANDS (Chemistry); PHOSPHATES; ULTRAVIOLET spectra; CHEMICAL bonds; METALLOPROTEINS
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2012, Vol 17, Issue 7, p1025
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-012-0916-x