A variable temperature spectroscopic study on Paracoccus pantotrophus pseudoazurin: Protein constraints on the blue Cu site

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Abstract

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 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 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 Cu2+-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 Cu2+-S-Cys bond. (C) 2009 Elsevier Inc. All rights reserved.
Original languageUnknown
Pages (from-to)1307-1313
JournalJournal of Inorganic Biochemistry
Volume103
Issue number10
DOIs
Publication statusPublished - 1 Jan 2009

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