ChemInform Abstract: Vibrational Relaxation in Carotenoids in Vivo and in Vitro: Picosecond Time-Resolved Anti-Stokes Resonance Raman Spectroscopy.

ChemInform ◽  
2010 ◽  
Vol 22 (49) ◽  
pp. no-no
Author(s):  
H. HAYASHI ◽  
T. L. BRACK ◽  
T. NOGUCHI ◽  
M. TASUMI ◽  
G. H. ATKINSON
Keyword(s):  
Raman Spectroscopy ◽  
Vibrational Relaxation ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Time Resolved ◽  
Anti Stokes

Vibrational relaxation in carotenoids in vivo and in vitro: picosecond time-resolved anti-Stokes resonance Raman spectroscopy

1991 ◽  
Vol 95 (18) ◽  
pp. 6797-6802 ◽  
Author(s):  
H. Hayashi ◽  
T. L. Brack ◽  
T. Noguchi ◽  
M. Tasumi ◽  
G. H. Atkinson
Keyword(s):  
Raman Spectroscopy ◽  
Vibrational Relaxation ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Time Resolved ◽  
Anti Stokes

Resonance Raman spectroscopy

2002 ◽  
Vol 06 (04) ◽  
pp. 301-302 ◽  
Author(s):  
Teizo Kitagawa
Keyword(s):  
Raman Spectroscopy ◽  
Heme Proteins ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Low Frequency ◽  
Time Resolved ◽  
Vibrational Assignments ◽  
Coherent Spectroscopy ◽  
Resonance Raman Spectra ◽  
Anti Stokes

The main topics in resonance Raman spectroscopy presented at ICPP-2 in Kyoto are briefly discussed. These include: (i) coherent spectroscopy and low frequency vibrations of ligand-photodissociated heme proteins, (ii) vibrational relaxation revealed by time-resolved anti-Stokes Raman spectroscopy, (iii) electron transfer in porphyrin arrays, (iv) vibrational assignments of tetraazaporphyrins and (v) resonance Raman spectra of an NO storing protein, nitrophorin.

scholarly journals The combination of resonance Raman spectroscopy, optical tweezers and microfluidic systems applied to the study of various heme-containing single cells

2008 ◽  
Vol 22 (4) ◽  
pp. 287-295 ◽  
Author(s):  
K. Ramser ◽  
W. Wenseleers ◽  
S. Dewilde ◽  
S. Van Doorslaer ◽  
L. Moens
Keyword(s):  
Raman Spectroscopy ◽  
Optical Tweezers ◽  
Single Cells ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Protective Role ◽  
Microfluidic Systems ◽  
Spectroscopy Optical

Several recent studies on the function of neuroglobin (Ngb), a hemoprotein predominantly expressed in the brain, point toward a neuro-protective role during hypoxic-ischemic injuries. The exact mechanism by which Ngb protects the cell against H2O2-induced cell death remains to be elucidated. Hence, new tools need to be developed in order to study the proteinin vivoor under physiological conditions. In this summary of our work, we demonstrate how resonance Raman spectroscopy, optical tweezers and microfluidic systems were combined to mimicin vivoconditions in anin vitromilieu. The setup has been tested on several globin-containing cells: hemoglobin (Hb) within single red blood cells (RBCs), a nerve globin present in the nerve cord of the annelidAphrodite aculeata(A. aculeata), and wild-type (wt) human neuroglobin (NGB) overexpressed inEscherichia coli(E. coli) bacteria. The feasibility of the setup regarding sensitivity and photo-induced effects and the results regarding the oxygen uptake and release will be discussed and compared for each system. The summary of the results show that the method is promising and the setup will be developed further to monitor the dependence of the neuronal action potential on nerve globins.

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