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

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

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Novel Chiroptical Analysis of Hemoglobin by Surface Enhanced Resonance Raman Optical Activity Spectroscopy. / Brazhe, Nadezda; Brazhe, Alexey; Sosnovtseva, Olga; Abdali, Salim.

In: Chirality, Vol. 21, No. 1E, 2010, p. E307-E312.

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

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Author

Brazhe, Nadezda; Brazhe, Alexey; Sosnovtseva, Olga; Abdali, Salim / Novel Chiroptical Analysis of Hemoglobin by Surface Enhanced Resonance Raman Optical Activity Spectroscopy.

In: Chirality, Vol. 21, No. 1E, 2010, p. E307-E312.

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

Bibtex

@article{ba3276d2b9ae4914bc10d01b00032cf4,
title = "Novel Chiroptical Analysis of Hemoglobin by Surface Enhanced Resonance Raman Optical Activity Spectroscopy",
keywords = "SEROA/SERROA, hemoglobin, chirality, SERS/SERRS, resonance raman spectroscopy",
publisher = "John/Wiley & Sons, Inc. John/Wiley & Sons Ltd.",
author = "Nadezda Brazhe and Alexey Brazhe and Olga Sosnovtseva and Salim Abdali",
year = "2010",
doi = "10.1002/chir.20820",
volume = "21",
number = "1E",
pages = "E307--E312",
journal = "Chirality",
issn = "0899-0042",

}

RIS

TY - JOUR

T1 - Novel Chiroptical Analysis of Hemoglobin by Surface Enhanced Resonance Raman Optical Activity Spectroscopy

A1 - Brazhe,Nadezda

A1 - Brazhe,Alexey

A1 - Sosnovtseva,Olga

A1 - Abdali,Salim

AU - Brazhe,Nadezda

AU - Brazhe,Alexey

AU - Sosnovtseva,Olga

AU - Abdali,Salim

PB - John/Wiley & Sons, Inc. John/Wiley & Sons Ltd.

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

KW - SEROA/SERROA

KW - hemoglobin

KW - chirality

KW - SERS/SERRS

KW - resonance raman spectroscopy

U2 - 10.1002/chir.20820

DO - 10.1002/chir.20820

JO - Chirality

JF - Chirality

SN - 0899-0042

IS - 1E

VL - 21

SP - E307-E312

ER -