In situ Raman study of redox state changes of mitochondrial cytochromes in a perfused rat heart
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In situ Raman study of redox state changes of mitochondrial cytochromes in a perfused rat heart. / Brazhe, Nadezda; Treiman, Marek; Faricelli, Barbara ; Vestergaard, Jakob Hedemark; Sosnovtseva, Olga.
In: PLOS ONE, Vol. 8, No. 8, 29.08.2013, p. e70488.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - In situ Raman study of redox state changes of mitochondrial cytochromes in a perfused rat heart
AU - Brazhe, Nadezda
AU - Treiman, Marek
AU - Faricelli, Barbara
AU - Vestergaard, Jakob Hedemark
AU - Sosnovtseva, Olga
PY - 2013/8/29
Y1 - 2013/8/29
N2 - We developed a Raman spectroscopy-based approach for simultaneous study of redox changes in c-and b-type cytochromes and for a semiquantitative estimation of the amount of oxygenated myoglobin in a perfused rat heart. Excitation at 532 nm was used to obtain Raman scattering of the myocardial surface of the isolated heart at normal and hypoxic conditions. Raman spectra of the heart under normal pO2 demonstrate unique peaks attributable to reduced c-and b-type cytochromes and oxymyoglobin (oMb). The cytochrome peaks decreased in intensity upon FCCP treatment, as predicted from uncoupling mitochondrial respiration. Conversely, transient hypoxia causes the reversible increase in the intensity of peaks assigned to cytochromes c and c1, reflecting electron stacking proximal to cytochrome oxidase due to the lack of terminal electron acceptor O2. Intensities of peaks assigned to oxy- and deoxyhemoglobin were used for the semiquantitative estimation of oMb deoxygenation that was found to be of approximately 50[Formula: see text] under hypoxia conditions.
AB - We developed a Raman spectroscopy-based approach for simultaneous study of redox changes in c-and b-type cytochromes and for a semiquantitative estimation of the amount of oxygenated myoglobin in a perfused rat heart. Excitation at 532 nm was used to obtain Raman scattering of the myocardial surface of the isolated heart at normal and hypoxic conditions. Raman spectra of the heart under normal pO2 demonstrate unique peaks attributable to reduced c-and b-type cytochromes and oxymyoglobin (oMb). The cytochrome peaks decreased in intensity upon FCCP treatment, as predicted from uncoupling mitochondrial respiration. Conversely, transient hypoxia causes the reversible increase in the intensity of peaks assigned to cytochromes c and c1, reflecting electron stacking proximal to cytochrome oxidase due to the lack of terminal electron acceptor O2. Intensities of peaks assigned to oxy- and deoxyhemoglobin were used for the semiquantitative estimation of oMb deoxygenation that was found to be of approximately 50[Formula: see text] under hypoxia conditions.
U2 - 10.1371/journal.pone.0070488
DO - 10.1371/journal.pone.0070488
M3 - Journal article
C2 - 24009655
VL - 8
SP - e70488
JO - PLoS ONE
JF - PLoS ONE
SN - 1932-6203
IS - 8
ER -
ID: 47711571