help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 38: 15-18 (1982)
© 1982 the Biophysical Society

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Reynolds, A H
Right arrow Articles by Rentzepis, P M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Reynolds, A H
Right arrow Articles by Rentzepis, P M

Kinetics and temperature dependence of carboxymyoglobin ligand photodissociation.

A H Reynolds and P M Rentzepis

ABSTRACT

We have observed the rate of oxymyoglobin (MbO2) photodissociation at room temperature and carboxymyoglobin (MbCO) photodissociation as a function of temperature (260-10 K) by means of picosecond spectroscopy. The Mb + O2 and Mb + CO photodissociated states have also been characterized. Based on the picosecond experimental data, we postulate that the photodissociation of ligated myoglobin is a nonactivitated process, and the mechanism involves either a small enthalpy barrier or none at all.




This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
U. Liebl, L. Bouzhir-Sima, M. Negrerie, J.-L. Martin, and M. H. Vos
Ultrafast ligand rebinding in the heme domain of the oxygen sensors FixL and Dos: General regulatory implications for heme-based sensors
PNAS, October 1, 2002; 99(20): 12771 - 12776.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1982 by the Biophysical Society.