Expand this Topic clickable element to expand a topic
Skip to content
Optica Publishing Group

Investigation of the Reaction Coordinate for Ligand Rebinding in Photoexcited Hemeproteins Using Transient Raman Spectroscopy

Not Accessible

Your library or personal account may give you access

Abstract

Picosecond two-color difference Raman spectroscopy is used to study the ultrafast photodeligation and the subsequent geminate recombination of oxyhemoglobin and carbonylhemoglobin. Complimentary Stokes and anti-Stokes spectra are used to distinguish vibrational cooling from structural changes in the heme. These structural changes are related to ligand dissociation and rebinding. Transient Raman spectra unambiguously show vibrational cooling and slow ligand rebinding in the hemeproteins. The deconvolved time constant of vibrational cooling is about 2-5 picoseconds.

© 1992 The Author(s)

PDF Article
More Like This
Ultrafast measurements of energy flow, geminate recombination, and fast structural rearrangements in photoexcited heme proteins

Huiping Zhu, Xiaobing Xu, Robert Lingle, and J. B. Hopkins
FJ2 OSA Annual Meeting (FIO) 1991

Protein Dynamics and Reactivity in Hemoglobin: Transient Raman and Picosecond Raman Hole Burning Studies

Blair F. Campbell and Joel M. Friedman
WA5 International Conference on Ultrafast Phenomena (UP) 1986

Direct observations of ligand rebinding trajectories in myoglobi by femtosecond mid-IR spectroscopy

Seongheun Kim and Manho Lim
ThC2 International Conference on Ultrafast Phenomena (UP) 2004

Select as filters


Select Topics Cancel
© Copyright 2024 | Optica Publishing Group. All rights reserved, including rights for text and data mining and training of artificial technologies or similar technologies.