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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
Author(s) -
Cavalu S.,
CîntăPînzaru S.,
Leopold N.,
Kiefer W.
Publication year - 2001
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10002
Subject(s) - chemistry , raman spectroscopy , bovine serum albumin , porphyrin , cytochrome c , raman scattering , cytochrome , resonance raman spectroscopy , surface enhanced raman spectroscopy , spectroscopy , serum albumin , adsorption , colloid , crystallography , analytical chemistry (journal) , photochemistry , chromatography , organic chemistry , biochemistry , enzyme , physics , quantum mechanics , optics , mitochondrion
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 α‐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. © 2001 John Wiley & Sons, Inc. Biopolymers (Biospectroscopy) 62: 341–348, 2001