کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1316812 | 976484 | 2009 | 7 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A variable temperature spectroscopic study on Paracoccuspantotrophus pseudoazurin: Protein constraints on the blue Cu site A variable temperature spectroscopic study on Paracoccuspantotrophus pseudoazurin: Protein constraints on the blue Cu site](/preview/png/1316812.png)
The blue or Type 1 (T1) copper site of Paracoccuspantotrophus pseudoazurin exhibits significant absorption intensity in both the 450 and 600 nm regions. These are σ and π SCys to Cu2+ charge transfer (CT) transitions. The temperature dependent absorption, EPR, and resonance Raman (rR) vibrations enhanced by these bands indicate that a single species is present at all temperatures. This contrasts the temperature dependent behavior of the T1 center in nitrite reductase [S. Ghosh, X. Xie, A. Dey, Y. Sun, C. Scholes, E. Solomon, Proc. Natl. Acad. Sci. 106 (2009) 4969–4974] which has a thioether ligand that is unconstrained by the protein. The lack of temperature dependence in the T1 site in pseudoazurin indicates the presence of a protein constraint similar to the blue Cu site in plastocyanin where the thioether ligand is constrained at 2.8 Å. However, plastocyanin exhibits only π CT. This spectral difference between pseudoazurin and plastocyanin reflects a coupled distortion of the site where the axial thioether in pseudoazurin is also constrained, but at a shorter Cu–SMet bond length. This leads to an increase in the Cu2+–SCys bond length, and the site undergoes a partial tetragonal distortion in pseudoazurin. Thus, its ground state wavefunction has both σ and π character in the Cu2+–SCys bond.
Journal: Journal of Inorganic Biochemistry - Volume 103, Issue 10, October 2009, Pages 1307–1313