Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy

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Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy. / Brazhe, Nadezda A; Brazhe, Alexey R; Sosnovtseva, Olga; Abdali, Salim.

I: Chirality, Bind 21 , Nr. 1E, 2010, s. E307-12.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Brazhe, NA, Brazhe, AR, Sosnovtseva, O & Abdali, S 2010, 'Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy', Chirality, bind 21 , nr. 1E, s. E307-12. https://doi.org/10.1002/chir.20820

APA

Brazhe, N. A., Brazhe, A. R., Sosnovtseva, O., & Abdali, S. (2010). Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy. Chirality, 21 (1E), E307-12. https://doi.org/10.1002/chir.20820

Vancouver

Brazhe NA, Brazhe AR, Sosnovtseva O, Abdali S. Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy. Chirality. 2010;21 (1E):E307-12. https://doi.org/10.1002/chir.20820

Author

Brazhe, Nadezda A ; Brazhe, Alexey R ; Sosnovtseva, Olga ; Abdali, Salim. / Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy. I: Chirality. 2010 ; Bind 21 , Nr. 1E. s. E307-12.

Bibtex

@article{78b7e710366111df8ed1000ea68e967b,

title = "Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy",

abstract = "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 nu(4), nu(20), and nu(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.",

author = "Brazhe, {Nadezda A} and Brazhe, {Alexey R} and Olga Sosnovtseva and Salim Abdali",

year = "2010",

doi = "10.1002/chir.20820",

language = "English",

volume = "21 ",

pages = "E307--12",

journal = "Chirality",

issn = "0899-0042",

publisher = "Wiley",

number = "1E",

}

RIS

TY - JOUR

T1 - Novel chiroptical analysis of hemoglobin by surface enhanced resonance Raman optical activity spectroscopy

AU - Brazhe, Nadezda A

AU - Brazhe, Alexey R

AU - Sosnovtseva, Olga

AU - Abdali, Salim

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 nu(4), nu(20), and nu(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.

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 nu(4), nu(20), and nu(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.

U2 - 10.1002/chir.20820

DO - 10.1002/chir.20820

M3 - Journal article

C2 - 20049977

VL - 21

SP - E307-12

JO - Chirality

JF - Chirality

SN - 0899-0042

IS - 1E

ER -

ID: 18787832