Hemoglobin resonance Raman

Friedman J M 1994 Time-resolved resonance Raman spectroscopy as probe of structure, dynamics, and reactivity in hemoglobin Methods Enzymol. 232 205-31... 

RESONANCE RAMAN SPECTROSCOPY HEMOGLOBIN BOHR EFFECT... 

HEMOGLOBINS POLYMERIZATION RESONANCE RAMAN SPECTROSCOPY HEMOGLOBIN-S POLYMERIZATION HENDERSON-HASSELBALCH EQUATION HENDERSON PLOT Henri-Brown treatment,... 

Franzen, S., Bohn, B., Poyart, C., and Martin, J. L. 1995. Evidence for sub-picosecond heme doming in hemoglobin and myoglobin A time-resolved resonance Raman comparison of carbonmonoxy and deoxy species. Biochemistry 34 1224-37. 

The use of picosecond pulses to minimize the Interference of fluorescence with the Raman spectrum was also demonstrated (5) at about that time. The use of vldicon detection in Raman spectroscopy was demonstrated (6) in 1976. The first resonance Raman spectrum taken for a photobiologlcal system (bacteriorhodopsin) in the nanosecond time scale was (7) in 1977. The resonance Raman spectra of bacteriorhodopsin have also been measured in the microsecond (8,9,10) and in the millisecond (11) time domain. Recently the time resolved resonance Raman spectra of photolyzed hemoglobin derivatives have been reported (12). 

Vander Meulen and Ressler (1980) measured the near-lR spectra of proteins in aqueous solution and compared them with the spectra of protein films. Brown et al. (1983) reported multiple internal reflectance spectra of hydrated films of carbonmonoxy and oxy forms of hemoglobin. This work was extended by Findsen et al. (1986), who, using resonance Raman scattering, measured the effects of hydration on the equilibrium and dynamic properties of hemoglobin and its carbonmonoxy complex. There was a substantial effect of hydration on the CO vibration, but no significant effect on the vibrational properties of the heme protein. 

Ackers GK, Holt JM. Asymmetric cooperativity in a symmetric tetramer human hemoglobin. J. Biol. Chem. 2006 281 11441-11443. Jayaraman V, Spiro TG. Structure of a third cooperativity state of hemoglobin ultraviolet resonance Raman spectroscopy of cyanome-themoglobin ligation microstates. Biochemistry 1995 34 4511 515. 

Double microscope configuration. One optical trap 830 nm, Raman, 488.0, 514.5, and 568.2 nm. One optical trap 1,064 nm, Raman 514.5 nm Hemoglobin (Hb) within red blood cells (RBCs) Oxidation state markers between 1,300 and 1,640 cm Different wavelengths for resonance Raman on Hb are investigated Oxygenation cycle of a red blood cell in a microfluidic system is demonstrated... 

Information about changes between different quaternary structures in the protein matrix of hemoglobin were obtained by Friedman et al.S9) and Lyons et al.62). The authors recorded resonance Raman spectra after photolysis of HbCO. They used a 10 ns Nd YAG laser pulse at 530 nm for photolysis and monitored the Raman spectra of the transient species (occurring within 10 ns after photolysis) with a N2-pumped dye laser. 

A variety of additional measurements have been made on the photolysis behavior of myoglobin and the related protein, hemoglobin. These include room-temperature transient electronic absorption studies in the nanosecond range,521 nanosecond-to-picosecond resonance Raman spectroscopy,522,523 and low-temperature transient electronic absorption measurements in regions other than the Soret band.524... 

As our kinetic picture matures, the spectroscopy of the intermediate states, whether by optical spectra (Hofrichter et al., 1983), Mossbauer (Marcolin et al., 1979), electron-spin resonance (Yonetani et al., 1974), or resonance Raman (Spiro, 1981 Ondrias et al., 1983) will allow a complete picture of the simple act of cooperativity in hemoglobin, and perhaps some idea of the role that the heme group plays in truly catalytic process in biology (Sligar and Gunsalus, 1979). 

Nakayama, S., F. Tani, M. Matsu-ura, and Y. Naruta (2002). Cobalt single-coronet porphyrin bearing hydroxyl groups in its 0-2 binding site as a new model for myoglobin and hemoglobin Observation of unusually low frequency of V(O-O) in resonance raman spectrum. Chem. Lett. 496 97. 

Perhaps the most important application of resonance Raman spectroscopy has been to the study ol biological molecules under physiologically significant conditions that is. in the presence of water and at low to moderate concentration levels.. - s an example, the technique has been useil lo determine the oxidation state and spin of iron atoms in hemoglobin and cytochrome c. In these molecules, the lesonance Raman bands are due solelv to ibrational modes of the tetra-... 

Fig. 18. Resonance Raman spectra of the (left) and (right) subunits of valency hybrid hemoglobins excited at 441.6 nm. (a) Isolated chain (pH 6.5) (b) stripped /nei-cyanide hybrid at pH 9.0 (c) mei-cyanide hybrid with inositol hexaphosphate (IHP) at pH 6.5 (d) stripped deoxyHb M Milwaukee at pH 6.5 (left) and stripped deoxyHb M Boston at pH 6.5 (right). All samples were in 50 mAf Bis-Tris/50 mAf Tris buffer. (From Nagai and Kitagawa. )...

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