Detection of nano-oxidation sites on the surface of hemoglobin crystals using tip-enhanced Raman scattering.
Hemoglobin nanocrystals were analyzed with tip-enhanced Raman scattering (TERS), surface-enhanced resonance Raman scattering (SERRS) and conventional resonance Raman scattering (RRS) using 532 nm excitation. The extremely high spatial resolution of TERS enables selective enhancement of heme, protein, and amino acid bands from the crystal surface not observed in the SERRS or RRS spectra. Two bands appearing at 1378 and 1355 cm(-1) assigned to the ferric and ferrous oxidation state marker bands, respectively, were observed in both TERS and SERRS spectra but not in the RRS spectrum of the bulk sample. The results indicate that nanoscale oxidation changes are occurring at the hemoglobin crystal surface. These changes could be explained by oxygen exchange at the crystal surface and demonstrate the potential of the TERS technique to obtain structural information not possible with conventional Raman microscopy.
Centre for Biospectroscopy, School of Chemistry, Monash University, 3800, Victoria, Australia. bayden.wood@monash.edu
Bayden R
BR
Wood
Mehdi
M
Asghari-Khiavi
Elena
E
Bailo
Don
D
McNaughton
Volker
V
Deckert
D001665:Binding Sites; D006454:Hemoglobins / Q000737:chemistry* / Q000648:ultrastructure*; D008422:Materials Testing / Q000379:methods; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D010084:Oxidation-Reduction; D011485:Protein Binding; D013059:Spectrum Analysis, Raman / Q000295:instrumentation* / Q000379:methods*; D013499:Surface Properties
D006454:Hemoglobins