1 May 1993 Probing the reaction coordinate for ligand binding in hemoglobin using ultrafast transient Raman spectroscopy
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Proceedings Volume 1890, Biomolecular Spectroscopy III; (1993) https://doi.org/10.1117/12.145250
Event: OE/LASE'93: Optics, Electro-Optics, and Laser Applications in Scienceand Engineering, 1993, Los Angeles, CA, United States
Abstract
Transient picosecond Raman spectroscopy is capable of differentiating vibrational relaxation from conformational changes by comparing the Stokes and anti-Stokes dynamics. We report pump-probe picosecond Raman experiments on oxy- and deoxyhemoglobin (oxyHb and deoxyHb, respectively) using 8 ps 532 nm pump pulses and 8 ps 355 nm probe pulses. Heme- to-protein vibrational cooling has been directly observed in deoxyHb for the first time, and the deconvolved cooling time constant is measured to be 2 - 5 ps. By applying our mode-specific Stokes and anti-Stokes technique to oxyHb, we find that any geminate recombination of photodeligated O2 must occur in either less than two picoseconds or longer than a nanosecond.
© (1993) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Huiping Zhu, Huiping Zhu, Robert Lingle, Robert Lingle, Xiaobing Xu, Xiaobing Xu, John B. Hopkins, John B. Hopkins, } "Probing the reaction coordinate for ligand binding in hemoglobin using ultrafast transient Raman spectroscopy", Proc. SPIE 1890, Biomolecular Spectroscopy III, (1 May 1993); doi: 10.1117/12.145250; https://doi.org/10.1117/12.145250
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