Share Email Print
cover

Proceedings Paper

Probing the reaction coordinate for ligand binding in hemoglobin using ultrafast transient Raman spectroscopy
Author(s): Huiping Zhu; Robert Lingle; Xiaobing Xu; John B. Hopkins
Format Member Price Non-Member Price
PDF $14.40 $18.00
cover GOOD NEWS! Your organization subscribes to the SPIE Digital Library. You may be able to download this paper for free. Check Access

Paper 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.

Paper Details

Date Published: 1 May 1993
PDF: 4 pages
Proc. SPIE 1890, Biomolecular Spectroscopy III, (1 May 1993); doi: 10.1117/12.145250
Show Author Affiliations
Huiping Zhu, Louisiana State Univ. (United States)
Robert Lingle, Louisiana State Univ. (United States)
Xiaobing Xu, Louisiana State Univ. (United States)
John B. Hopkins, Louisiana State Univ. (United States)


Published in SPIE Proceedings Vol. 1890:
Biomolecular Spectroscopy III
Laurence A. Nafie; Henry H. Mantsch, Editor(s)

© SPIE. Terms of Use
Back to Top