The Valence and Spin State of Iron in Oxyhemoglobin as Inferred from Resonance Raman Spectroscopy

Yamamoto, Tomoko; Palmer, Graham; Gill, D.; Salmeen, Irving T.; Rimai, L.

doi:10.1016/s0021-9258(19)43692-2

Cited by 191 publications

(74 citation statements)

References 18 publications

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“…Their results showed that iron in oxygenated hemoglobin exists in the low-spin ferric (Fe 3+ ) state rather than the low-spin ferrous (Fe 2+ ) state. 19 The following year, Spiro and Strekas published important work on the spin state of the central iron atom, 20 and Woodruff and Spiro later published a report that described a sample cell that allowed different forms of hemoglobin to circulate while spectra were being collected (thereby reducing absorption and photo-damage). 21…”

Section: Applicationsmentioning

confidence: 99%

Raman Spectroscopy of Blood and Blood Components

et al. 2017

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Blood is a bodily fluid that is vital for a number of life functions in animals. To a first approximation, blood is a mildly alkaline aqueous fluid (plasma) in which a large number of free-floating red cells (erythrocytes), white cells (leucocytes), and platelets are suspended. The primary function of blood is to transport oxygen from the lungs to all the cells of the body and move carbon dioxide in the return direction after it is produced by the cells' metabolism. Blood also carries nutrients to the cells and brings waste products to the liver and kidneys. Measured levels of oxygen, nutrients, waste, and electrolytes in blood are often used for clinical assessment of human health. Raman spectroscopy is a nondestructive analytical technique that uses the inelastic scattering of light to provide information on chemical composition, and hence has a potential role in this clinical assessment process. Raman spectroscopic probing of blood components and of whole blood has been on-going for more than four decades and has proven useful in applications ranging from the understanding of hemoglobin oxygenation, to the discrimination of cancerous cells from healthy lymphocytes, and the forensic investigation of crime scenes. In this paper, we review the literature in the field, collate the published Raman spectroscopy studies of erythrocytes, leucocytes, platelets, plasma, and whole blood, and attempt to draw general conclusions on the state of the field.

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Section: Applicationsmentioning

confidence: 99%

Raman Spectroscopy of Blood and Blood Components

et al. 2017

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“…It has been demonstrated that Raman spectroscopy can be used for detection and quantification of heme and heme degradation products (a survey can be found in Neugebauer et al 8 ). With the exception of our sample line at 1399 cm -1 , none of the lines shown in the spectra of Yamamoto (hemoproteins), 9 Lu (methemoglobin), 10 or Zhu (pure blood and poisoning blood), 11 Ramser (human Hb), 12 and Wood and McNaughton 13 (oxygenated and deoxygenated hemoglobin) are present in our sample excited at 514.5 nm.…”

Section: Hemoglobin or Methemoglobin Hypothesismentioning

confidence: 57%

Raman and Energy Dispersive Spectroscopy (EDS) Analyses of a Microsubstance Adhering to a Fiber of the Turin Shroud

Laude

Fanti

2017

Appl Spectrosc

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The Raman spectrum of a microsubstance, smeared on a fiber coming from the Shroud of Turin, was compared with numerous spectra published for old or modern pigment dyes, whole bloods, dried bloods, red blood cells, albumin, very ancient blood stains, and various "degradation" products of heme. Within the wavenumber measure accuracy, it is shown that all Raman lines detected above background could correspond to vibration frequencies found in biliverdin-derived compounds except a weak line that we tentatively attributed to amide I. Biliverdin is known as an oxidative ring cleavage product of the heme of blood. Energy dispersive spectroscopy (EDS) analysis of the sample confirms an elemental composition fully compatible with this hypothesis. Therefore, it is very likely that this microsubstance contains products of heme including heme/biliverdin-derived compounds and protein traces (amide I). Nevertheless, other measures will be necessary to confirm it. This method of identification, adding EDS to Raman spectrometry can be applied to nondestructive testing (NDT) of many other microsamples.

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“…100 cm-1 lower than th a t of singlet 0 2, a decrease similar to th a t observed for CO on binding to Hb (Alben & Caughey 1968). Yamamoto et al (1973) observed th a t the 1375 cm-1 haem resonance Ram an frequency appears to be an indicator of oxidation state, and th a t 0 2Hb classifies as Fe h i in line with Weiss' (1964) model. This classification was confirmed by Spiro and Strekas (1974), who also found, however, th a t COHb classifies similarly, and pointed out th a t back-bonding to 0 2 or CO could account for the Ram an frequencies without an actual superoxide (or CO-) radical being involved.…”

Section: ( D) Electron Distribution To Oxyhaemoglobinmentioning

confidence: 61%

“…Essentially insensitive to spin-state changes, this band decreases from 1375 cm-1 for Fe 111 haems to ca. 1360 cm-1 for Fe 11 haems (Yamamoto et al 1973).…”

Section: R E S O N a N C E R A M A N S C A T T E R I N Gmentioning

confidence: 93%

Biological applications of resonance Raman spectroscopy: haem proteins

Spiro

1975

Proc. R. Soc. Lond. A

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Resonance Raman spectroscopy involves laser excitation within an absorption band of the sample. Certain vibrational modes, those which couple to the electronic transition, exhibit greatly increased Raman scattering in the resulting spectrum. Sensitivity approaches that of absorption spectrophotometry, while the high resolution characteristic of vibrational spectroscopy is preserved, even in solution at room temperature. If the resonant electronic transition is associated with a site of biological activity, then the technique offers a sensitive probe for structural features of the site. Haem proteins afford particularly informative resonance Raman spectra, with a rich assortment of porphyrin ring vibrations, which can be classified and analysed via their symmetry properties. Certain of these frequencies are sensitive to the structural concomitants of spin- and oxidation-state changes of the haem group. These can be used to monitor the structural consequences of ligation or electron transfer in haem proteins.

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The Valence and Spin State of Iron in Oxyhemoglobin as Inferred from Resonance Raman Spectroscopy

Cited by 191 publications

References 18 publications

Raman Spectroscopy of Blood and Blood Components

Raman Spectroscopy of Blood and Blood Components

Raman and Energy Dispersive Spectroscopy (EDS) Analyses of a Microsubstance Adhering to a Fiber of the Turin Shroud

Biological applications of resonance Raman spectroscopy: haem proteins

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