Biomedical Application of Near-Infrared Fourier Transform Raman Spectroscopy. Part I: The 1064-nm Excited Raman Spectra of Blood and Met Hemoglobin

A resonance Raman spectroscopic investigation into the effects of fixation and dehydration on heme environment of hemoglobin

“…This band is tentatively assigned to an amide III band based on an earlier study. [27] The RR spectra of hemichrome and dried RBCs are almost superimposable (Fig. 2) demonstrating that Hb in air-dried RBCs changes to a low-spin six coordinate Fe III component, hemichrome.…”

Raman Spectroscopy of Blood and Blood Components

“…The spectra showed that the amide I band had shifted, an indication that hemoglobin was denatured (a-helix structures becoming random coil structures). 34 In 1997, related work by Schrader et al would demonstrate the obvious similarities between Raman features of whole blood and those of erythrocytes ( Figure 13). 199 Ozaki and colleagues would later use three separate excitation wavelengths (514.5 nm, 720 nm, and 1064 nm) on samples of whole blood and isolated hemoglobin to determine that the 720 nm excitation yielded strong Raman scattering of carotenoids and protein.…”

“…Thus, with $150 g of highly scattering hemoglobin in each liter of whole blood, it is no surprise that the metalloprotein dominates the Raman spectrum and makes analysis of other chemical species difficult. 34 The difficulty has not deterred workers from undertaking Raman analysis of whole blood, however; in 1992 Ozaki et al used FT-Raman (1064 nm excitation) to obtain a spectrum of whole blood and compared the result to that of coagulated (via laser irradiation) whole blood. The spectra showed that the amide I band had shifted, an indication that hemoglobin was denatured (a-helix structures becoming random coil structures).…”

“…Ozaki et al deployed near-infrared (NIR) Fourier transform (FT) Raman spectroscopy (1064 nm excitation) to study met-hemoglobin (metHb), a form of hemoglobin that contains iron in the Fe 3þ state but cannot bind oxygen. 34 Later, the Spiro group chemically altered sub-unit regions of hemoglobin that they suspected to be important to the protein's quaternary structure (they removed C-terminus residues from particular amino acids) and used two different RRS excitations (229 nm and 441.6 nm) to show the alterations increased hemoglobin's oxygen affinity and affected its functionality (the alterations reduced the protein's Bohr effect and its cooperativity). 35 Raman spectroscopy analyses of isolated hemoglobin and its many variants 36 have led to deeper understanding of the metalloprotein's form and function.…”

Micro-Raman Spectroscopy Monitor Methemoglobin Induced by Sodium Nitrite in Whole Blood

“…Raman spectroscopy has been utilized in studies of biological media, and can characterize tissues [5][6][7]. Ozaki et al obtained information about hemoglobin in blood by the near-infrared FT-Raman spectroscopy [8]. Concentrations of multiple analytes such as glucose, urea, albumin, triglycerides, hematocrit, and hemoglobin were simultaneously measured in whole blood using near-infrared Raman spectroscopy [9][10].…”