@article {2290,
	title = {A variable temperature spectroscopic study on Paracoccus pantotrophus pseudoazurin: Protein constraints on the blue Cu site},
	journal = {Journal of Inorganic Biochemistry},
	volume = {103},
	number = {10},
	year = {2009},
	note = {<p>Times Cited: 2Si1st Latin American Meeting on Biological Inorganic Chemistry (LABIC2008)Aug 31-sep 04, 2008Iguazu Falls, BRAZIL</p>
},
	month = {Oct},
	pages = {1307-1313},
	abstract = {<p>The blue or Type 1 (T1) copper site of Paracoccus pantotrophus pseudoazurin exhibits significant absorption intensity in both the 450 and 600 nm regions. These are sigma and pi S(Cys) to Cu(2+) 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 angstrom. However, plastocyanin exhibits only pi CT. This spectral difference between pseudoazurin and plastocyanin reflects a coupled distortion of the site where the axial thiorether in pseudoazurin is also constrained, but at a shorter Cu-S(Met) bond length. This leads to an increase in the Cu(2+)-S(Cys) bond length, and the site undergoes a partial tetragonal distortion in pseudoazurin. Thus, its ground state wavefunction has both sigma and pi character in the Cu(2+)-S(Cys) bond. (C) 2009 Elsevier Inc. All rights reserved.</p>
},
	isbn = {0162-0134},
	url = {http://dx.doi.org/10.1016/j.jinorgbio.2009.04.012},
	author = {Xie, Xiangjin and Hadt, Ryan G. and Pauleta, Sofia R. and Gonzalez, Pablo J. and Un, Sun and Moura, Isabel and Solomon, Edward I.}
}
