title: Raman and surface enhanced Raman spectroscopy of 2,2,5,5-tetramethyl-3-pyrrolin-1-yloxy-3-carboxamide labeled proteins: bovine serum albumin and cytochrome c.
abstract: 2,2,5,5-Tetramethyl-3-pyrrolin-1-yloxy-3-carboxamide (tempyo) labeled bovine serum albumin and cytochrome c at different pH values were prepared and investigated using Raman-resonance Raman (RR) spectroscopy and surface enhanced Raman scattering (SERS) spectroscopy. The Raman spectra of tempyo labeled proteins in the pH 6.7-11 range were compared to those of the corresponding free species. The SERS spectra were interpreted in terms of the structural changes of the tempyo labeled proteins adsorbed on the silver colloidal surface. The tempyo spin label was found to be inactive in the Raman-RR and SERS spectra of the proteins. The alpha-helix conformation was concluded to be more favorable as the SERS binding site of bovine serum albumin. In the cytochrome c the enhancement of the bands assigned to the porphyrin macrocycle stretching mode allowed the supposition of the N-adsorption onto the colloidal surface.
authors.affiliation: Biophysics Department, University of Oradea, 1 Dec. Square, Number 10, RO-3700 Oradea, Romania. meda@medanet.ro
authors.forename: S
authors.initials: S
authors.lastname: Cavalu
authors.forename: S
authors.initials: S
authors.lastname: Cîntă-Pînzaru
authors.forename: N
authors.initials: N
authors.lastname: Leopold
authors.forename: W
authors.initials: W
authors.lastname: Kiefer
mesh_terms: D000818:Animals; D002417:Cattle; D003497:Cyclic N-Oxides; D003574:Cytochrome c Group / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D017433:Protein Structure, Secondary; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013059:Spectrum Analysis, Raman / Q000379:methods; D013113:Spin Labels
chemical_list: D003497:Cyclic N-Oxides; D003574:Cytochrome c Group; D013113:Spin Labels; D012710:Serum Albumin, Bovine; C047253:3-carbamoyl-2,2,5,5-tetramethyl-3-pyrroline-1-yloxyl