Resonance Raman spectroscopy hemoglobin

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,... 

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. 

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... 

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-... 

Static resonance Raman spectroscopy has emerged as an important and powerful method for investigating details of structure in compounds with strong absorption bands, such as hemoglobin (see, for example Asher [15]), and these advantages have been extended to kinetic studies by Dr. T.G. Spiro of Princeton, and Dr. J.M. Friedman of Bell Laboratories. It seems unlikely at present that their methods will... 

Wang, D.J., Spiro, T.G. Stmcture changes in hemoglobin upon deletion of C-terminal residues, monitored by resonance Raman spectroscopy. Biochemistry 37, 9940-9951 (1998)... 

Hu, X.H., Rodgers, K.R., Mukerji, I., Spiro, T.G. New light on allostery dynamic resonance Raman spectroscopy of hemoglobin Kempsey. Biochemistry 38, 3462-3467 (1999)... 

Zhao X and Spiro TG (1998) Ultraviolet resonance Raman spectroscopy of hemoglobin with 200 and 212 nm excitation H-bonds of tyrosines and prolines. Journal of Raman Spectroscopy 29 49-55. 

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). 

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). 

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