1973
DOI: 10.1016/0005-2795(73)90004-4
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Resonance Raman scattering on haemoglobin

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Cited by 87 publications
(58 citation statements)
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“…17 In follow-up work, Brunner used an oxygen isotope to identify a mode assignable to stretching of the iron-oxygen (Fe-O 2 ) bond at 567 cm À1 (Figure 2). 18 Understanding the nature of the Fe-O 2 bond was thought to be vital to the elucidation of oxygen binding in hemoglobin, and it became the subject of much research.…”
mentioning
confidence: 99%
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“…17 In follow-up work, Brunner used an oxygen isotope to identify a mode assignable to stretching of the iron-oxygen (Fe-O 2 ) bond at 567 cm À1 (Figure 2). 18 Understanding the nature of the Fe-O 2 bond was thought to be vital to the elucidation of oxygen binding in hemoglobin, and it became the subject of much research.…”
mentioning
confidence: 99%
“…38 Raman Spectroscopy Studies of Intact Red Blood Cells Intracellular Hemoglobin. In one of the early Brunner and Sussner studies mentioned above, 17 the investigators compared the spectrum of hemoglobin to the spectrum of intact RBCs and stated that ''the recorded Raman spectra of erythrocytes were identical to that of oxy-and deoxyHb, respectively, when we used the original suspension or added a small amount of deoxygenating dithionite''. 17 In 2001, almost thirty years after the original report, workers at Monash University in Victoria, Australia used conventional Raman spectroscopy (633 nm excitation) to record the same oxyHb (R state) and deoxyHb (T state) spectral features inside single living erythrocytes.…”
mentioning
confidence: 99%
“…In terms of HbO 2 Sat determination, this method has the advantage that the oxygenation information is related only to the specific interaction of the photons with the Hb molecules, generating a unique Raman spectrum (6,7,12,36,40,41). The vibrational bands of heme are well known (1,5), and previous Raman investigations of Hb have been carried out on isolated and purified Hb or in isolated red blood cells (27,33,34).…”
mentioning
confidence: 99%
“…If the Raman excitation wavelength matches a transition wavelength of the molecule, a selective resonance enhancement of the porphyrin Raman signal occurs, without spectral interference from the surrounding protein. 37,38 A process within RBCs that is well-known to be sensitive to photo-dissociation is the binding of oxygen to Hb. 39 The Raman bands at 1640 cm À1 , 1582 cm À1 , and 1378 cm À1 are characteristic for the oxygenated form of human hemoglobin (oxyHb) and undergo a shift to 1604 cm À1 , 1553 cm À1 , and 1355 cm À1 upon transition to the deoxygenated form (deoxyHb).…”
Section: Rbc Diffusive Behavior and Membrane Edge Fluctuationsmentioning
confidence: 99%