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

Biophysical Journal 49: 1195-1198 (1986)
© 1986 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 Wajnberg, E
Right arrow Articles by Helman, J S
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wajnberg, E
Right arrow Articles by Helman, J S

Spin relaxation of iron in mixed state hemoproteins.

E Wajnberg, H J Kalinowski, G Bemski and J S Helman

ABSTRACT

In hemoproteins the relaxation mechanism of iron is Orbach for high spin (HS) and Raman for low spin (LS). We found that in met-hemoglobin and met-myoglobin, under conditions in which the two spin states coexist, both the HS and the LS states relax to the lattice through Orbach-like processes. Alos, very short (approximately 1 ns) and temperature independent transverse relaxation times T2 were estimated. This may result from the unusual electronic structure of mixed states hemoproteins that allows thermal equilibrium and interconversion of the spin states.






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1986 by the Biophysical Society.