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

Biophysical Journal 52: 885-889 (1987)
© 1987 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 Google Scholar
Google Scholar
Right arrow Articles by Guest, C R
Right arrow Articles by Noe, L J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Guest, C R
Right arrow Articles by Noe, L J

Photodissociation of CO and O2 from alpha and beta hemoglobin chains studied by using picosecond absorption spectroscopy.

C R Guest and L J Noe

Department of Chemistry, University of Wyoming, Laramie 82071.

ABSTRACT

The picosecond photodissociation of the CO and O2 forms of alpha and beta chains of hemoglobin were studied by following pi pi Soret absorption changes using a Nd3+ phosphate-glass laser, 531-nm pump pulse, 8 ps full width half maximum, and a pump-probe double-beam absorption apparatus. Three intermediates were observed within the first 50 ps after photon absorption. The most notable differences between the two monomers are the extent and rate of geminate recombination with the two ligands. We attribute this result to differences between the tertiary protein structure of the alpha and beta forms of Hb, both distal and proximal.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1987 by the Biophysical Society.