| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 265, Issue 27, 16054-16059, 09, 1990
DW Kraus, JB Wittenberg, JF Lu and J Peisach
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461.
We report an optical and EPR spectral study of three hemoglobins, Hb I, II, and III, from the gill of the clam Lucina pectinata. Hemoglobin I reacts much more avidly with hydrogen sulfide than do Hbs II and III. The proximal ligand to the heme iron of each hemoglobin is histidyl imidazole. The acid/alkaline transition of ferric Hb I occurs with pK 9.6; those of ferric Hbs II and III with pK 6.6 and 5.9, respectively. At their acid limits each ferric hemoglobin exists as aquoferric hemoglobin. Broadening of the g = 6 resonance suggests that the bound water enjoys great positional freedom. Ferric Hb I, at the alkaline limit (pH 11), exists as ferric hemoglobin hydroxide. Ferric Hbs II and III, at their alkaline limit (pH 7.5), each exist as equal mixtures of two species. The low spin species with optical maxima near 541 and 576 nm and g values of 2.61, 2.20, and 1.82, are identified as ferric hemoglobin hydroxide. The high spin species, with optical maxima near 486 and 603 nm and g values of 6.71, 5.87, and 5.06, resemble Dicrocoelium hemoglobin and hemoglobin MSaskatoon. Here we show that Hbs II and III resemble hemoglobin MSaskatoon in which a distal tyrosinate oxygen ligated to the ferric heme iron at alkaline pH is displaced by water at acid pH. The H2S product of ferric Hb I is identified as ferric hemoglobin sulfide.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  J. A. Gavira, A. Camara-Artigas, W. De Jesus-Bonilla, J. Lopez-Garriga, A. Lewis, R. Pietri, S.-R. Yeh, C. L. Cadilla, and J. M. Garcia-Ruiz Structure and Ligand Selection of Hemoglobin II from Lucina pectinata J. Biol. Chem., April 4, 2008; 283(14): 9414 - 9423. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Caillet-Saguy, P. Turano, M. Piccioli, G. S. Lukat-Rodgers, M. Czjzek, B. Guigliarelli, N. Izadi-Pruneyre, K. R. Rodgers, M. Delepierre, and A. Lecroisey Deciphering the Structural Role of Histidine 83 for Heme Binding in Hemophore HasA J. Biol. Chem., February 29, 2008; 283(9): 5960 - 5970. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Fernandez-Alberti, D. E. Bacelo, R. C. Binning Jr., J. Echave, M. Chergui, and J. Lopez-Garriga Sulfide-Binding Hemoglobins: Effects of Mutations on Active-Site Flexibility Biophys. J., September 1, 2006; 91(5): 1698 - 1709. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. E. Weber and S. N. Vinogradov Nonvertebrate Hemoglobins: Functions and Molecular Adaptations Physiol Rev, April 1, 2001; 81(2): 569 - 628. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Couture, T. K. Das, H. C. Lee, J. Peisach, D. L. Rousseau, B. A. Wittenberg, J. B. Wittenberg, and M. Guertin Chlamydomonas Chloroplast Ferrous Hemoglobin. HEME POCKET STRUCTURE AND REACTIONS WITH LIGANDS J. Biol. Chem., March 12, 1999; 274(11): 6898 - 6910. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. K. Rashid, M.-L. Van Hauwaert, M. Haque, A. H. Siddiqi, I. Lasters, M. De Maeyer, N. Griffon, M. C. Marden, S. Dewilde, J. Clauwaert, et al. Trematode Myoglobins, Functional Molecules with a Distal Tyrosine J. Biol. Chem., January 31, 1997; 272(5): 2992 - 2999. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. Zhang, K. A. Rashid, M. Haque, A. H. Siddiqi, S. N. Vinogradov, L. Moens, and G. N.L. Mar Solution of 1H NMR Structure of the Heme Cavity in the Oxygen-avid Myoglobin from the Trematode Paramphistomum epiclitum J. Biol. Chem., January 31, 1997; 272(5): 3000 - 3006. [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 |
