Fourier transform Raman approach to structural correlation in hemoglobin derivatives
Autor: | Balan Venkatesh, S Ramasamy, Joseph M. Rifkind, M. Mylrajan, P. T. Manoharan, R Asokan |
---|---|
Rok vydání: | 1999 |
Předmět: |
Spin states
Protein Conformation Analytical chemistry Protoporphyrins chemistry Spectrum Analysis Raman Spectral line fluoro methemoglobin Analytical Chemistry chemistry.chemical_compound symbols.namesake Hemoglobins Oxidation state Nickel Spectroscopy Fourier Transform Infrared Humans Raman spectrometry Globin human infrared spectroscopy Instrumentation oxyhemoglobin Spectroscopy comparative study Methemoglobin Fourier Analysis deoxyhemoglobin fluoro-methemoglobin Near-infrared spectroscopy Resonance methodology hemoglobin cyanomethemoglobin Porphyrin Atomic and Molecular Physics and Optics Carboxyhemoglobin Oxyhemoglobins drug derivative symbols protoporphyrin Raman spectroscopy |
Zdroj: | Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy. (7-8) |
ISSN: | 1386-1425 |
Popis: | In order to obtain information on the structural aspects of hemoglobin (Hb), Fourier transform Raman (FT-R) measurements on various ferrous, ferric derivatives and nickel reconstituted Hb (NiHb) has been made. FT-R spectra for these derivatives were obtained by laser excitation in the near infrared region (NIR) (1064 nm) whereby the wave-number region (600-1700 cm-1) related to both porphyrin ring modes and some globin modes were monitored. Comparison of various modes was made based on previous resonance Raman (RR) results. The wave-number shifts with respect to changes in oxidation state and spin state are very similar to those observed by RR. Additional bands at 1654, 1459, and 1003 cm-1 for deoxyHb and at 1656, 1454, and 1004 cm-1 for oxy Hb can be correlated to globin modes. The shift in the position of these bands for the binding of oxygen can be related to changes in conformation during the transformation. The presence of two distinct sites in NiHb could be monitored by the use of FT-R technique. ? 1999 Elsevier Science B.V. All rights reserved. |
Databáze: | OpenAIRE |
Externí odkaz: |