Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Qiu, Y.
Right arrow Articles by Riggs, A. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Qiu, Y.
Right arrow Articles by Riggs, A. F.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 18, 13517-13528, May 5, 2000

Lamprey Hemoglobin
STRUCTURAL BASIS OF THE BOHR EFFECT*

Yang QiuDagger §, David H. Maillett, James Knapp||**, John S. Olson, and Austen F. RiggsDagger Dagger Dagger

From the Dagger  Section of Neurobiology, School of Biological Sciences and Institute for Molecular and Cell Biology, University of Texas, Austin, Texas 78712-1064, the  Department of Biochemistry and Cell Biology and the Keck Center for Computational Biology, Rice University, Houston, Texas 77005-1892, and the || Department of Chemistry and Biochemistry, University of Texas, Austin, Texas 78712-1167

Lampreys, among the most primitive living vertebrates, have hemoglobins (Hbs) with self-association and ligand-binding properties very different from those that characterize the alpha 2beta 2 tetrameric Hbs of higher vertebrates. Monomeric, ligated lamprey Hb self-associates to dimers and tetramers upon deoxygenation. Dissociation to monomers upon oxygenation accounts for the cooperative binding of O2 and its pH dependence. Honzatko and Hendrickson (Honzatko, R. B., and Hendrickson, W. A. (1986) Proc. Natl. Acad. Sci. U. S. A 83, 8487-8491) proposed that the dimeric interface of the Hb resembles either the alpha 1beta 2 interface of mammalian Hbs or the contacts in clam Hb where the E and F helices form the interface. Perutz (Perutz, M. F. (1989) Quart. Rev. Biophys. 2, 139- 236) proposed a version of the clam model in which the distal histidine swings out of the heme pocket upon deoxygenation to form a bond with a carboxyl group of a second monomer. The sedimentation behavior and oxygen equilibria of nine mutants of the major Hb component, PMII, from Petromyzon marinus have been measured to test these models. The results strongly support a critical role of the E helix and the AB corner in forming the subunit interface in the dimer and rule out the alpha 1beta 2 model. The pH dependence of both the sedimentation equilibrium and the oxygen binding of the mutant E75Q indicate that Glu75 is one of two groups responsible for the Bohr effect. Changing the distal histidine 73 to glutamine almost completely abolishes the self-association of the deoxy-Hb and causes a large increase in O2 affinity. The recent x-ray crystallographic determination of the structure of deoxy lamprey Hb, reported after the completion of this work (Heaslet, H. A., and Royer, W. E. (1999) Structure 7, 517-526), shows that the dimer interface does involve the E helix and the AB corner, supporting the measurements and interpretations reported here.

* This work was supported by National Science Foundation Grants MCB 951179 and 972385 (to A. F. R.), National Institutes of Health Grants GM 35649 and HL 47020 (to J. S. O.), and National Institutes of Health Biotechnology Training Grant T32-GM08362. Portions of this paper are based on a Ph.D. dissertation of Y. Qiu at the University of Texas at Austin, December, 1997. A preliminary account of the results has been presented (1).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF248645.

§ Present address: Functional Genomics Department, Lawrence Berkeley National Laboratory, 1 Cyclotron Rd., MS84-171, Berkeley, CA 94720.

** Present address: Dept. of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01655.

Dagger Dagger To whom correspondence should be addressed. Tel.: 512-471-1585; Fax: 512-471-9651; E-mail: riggs@uts.cc.utexas.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 ScienceHome page
M. Berenbrink, P. Koldkjaer, O. Kepp, and A. R. Cossins
Evolution of Oxygen Secretion in Fishes and the Emergence of a Complex Physiological System
Science, March 18, 2005; 307(5716): 1752 - 1757.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Mito, K. T. Chong, G. Miyazaki, S.-i. Adachi, S.-Y. Park, J. R. H. Tame, and H. Morimoto
Crystal Structures of Deoxy- and Carbonmonoxyhemoglobin F1 from the Hagfish Eptatretus burgeri
J. Biol. Chem., June 7, 2002; 277(24): 21898 - 21905.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. Ceci, L. Giangiacomo, A. Boffi, and E. Chiancone
The Mutation K30D Disrupts the Only Salt Bridge at the Subunit Interface of the Homodimeric Hemoglobin from Scapharca inaequivalvis and Changes the Mechanism of Cooperativity
J. Biol. Chem., February 22, 2002; 277(9): 6929 - 6933.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Fago, L. Giangiacomo, R. D'Avino, V. Carratore, M. Romano, A. Boffi, and E. Chiancone
Hagfish Hemoglobins. STRUCTURE, FUNCTION, AND OXYGEN-LINKED ASSOCIATION
J. Biol. Chem., July 13, 2001; 276(29): 27415 - 27423.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. A. Heaslet and W. E. Royer Jr.
Crystalline Ligand Transitions in Lamprey Hemoglobin. STRUCTURAL EVIDENCE FOR THE REGULATION OF OXYGEN AFFINITY
J. Biol. Chem., July 6, 2001; 276(28): 26230 - 26236.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement