Novel Chiroptical Analysis of Hemoglobin by Surface Enhanced Resonance Raman Optical Activity Spectroscopy

Publication: Research - peer-reviewJournal article – Annual report year: 2010

NullPointerException

View graph of relations

The metalloprotein hemoglobin (Hb) was studied using surface enhanced resonance Raman spectroscopy (SERRS) and surface enhanced resonance Raman optical activity (SERROA). The SERROA results are analyzed and compared with the SERRS, and the later to the resonance Raman (RRS) performed on Hb. The SERRS measurements careful optimization, with respect to the concentration and volume ratio of the analyte to colloids, enables for the first time SERROA of this molecule. We observed that the most intense SERROA signals were attributed the v(4), v(20), and v(21) vibrations, which are sensitive to the redox state of the heme's iron ion, and to the presence of its sixth site, bound to exogenous ligand; O-2, NO or CO. However, in this study, the SERROA signals corresponding to these vibrations appear more sensitive to the Hb oxygen-binding properties than they appear in the SERRS or RRS. Moreover, the SERROA signal of Hb has successfully been monitored as a function of time, and was observed to be stable for 4-5 min. To our knowledge, the SERROA results of Hb, and its comparison to SERRS and RRS, are here reported for the first time. Chirality 21:E307-E312, 2009.
Original languageEnglish
JournalChirality
Publication date2010
Volume21
Journal number1E
PagesE307-E312
ISSN0899-0042
DOIs
StatePublished
CitationsWeb of Science® Times Cited: 1

Keywords

  • SEROA/SERROA, hemoglobin, chirality, SERS/SERRS, resonance raman spectroscopy
Download as:
Download as PDF
Select render style:
APAAuthorCBEHarvardMLAStandardVancouverShortLong
PDF
Download as HTML
Select render style:
APAAuthorCBEHarvardMLAStandardVancouverShortLong
HTML
Download as Word
Select render style:
APAAuthorCBEHarvardMLAStandardVancouverShortLong
Word

ID: 5159254