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Blood, 15 January 2008, Vol. 111, No. 2, pp. 932-938. Prepublished online as a Blood First Edition Paper on October 17, 2007; DOI 10.1182/blood-2007-07-100180. This Article Full Text (PDF) All Versions of this Article: blood-2007-07-100180v1 111/2/932    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Chu, H. Articles by Low, P. S Search for Related Content PubMed PubMed Citation Articles by Chu, H. Articles by Low, P. S Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted July 13, 2007 Accepted October 13, 2007 Characterization of the deoxyhemoglobin binding site on human erythrocyte band 3: implications for O2 regulation of erythrocyte properties Haiyan Chu, Andrew Breite, Peter Ciraolo, Robert S Franco, and Philip S Low* Department of Chemistry, Purdue University, West Lafayette, IN, United States Division of Hematology/Oncology, University of Cincinnati College of Medicine, The Vontz Center for Molecular Studies, Cincinnati, OH, United States * Corresponding author; email: plow{at}purdue.edu. Band 3, the major protein of the human erythrocyte membrane, associates with multiple metabolic, ion transport, and structural proteins. Functional studies demonstrate that the oxygenation state of the erythrocyte regulates cellular properties performed by these and/or related proteins. Because deoxyhemoglobin, but not oxyhemoglobin, binds band 3 reversibly with high affinity, these observations raise the hypothesis that hemoglobin might regulate erythrocyte properties through its reversible, oxygenation-dependent association with band 3. To explore this hypothesis, we have characterized the binding site of deoxyHb on human erythrocyte band 3. We report that: i) deoxyHb binds to residues 12-23 of band 3; ii) mutation of residues on either side of this sequence greatly enhances affinity of deoxyHb for band 3, suggesting that evolution of a higher affinity interaction would have been possible had it been beneficial for survival; iii) Hb does not bind to two other sequences in band 3 despite their high sequence homology to residues 12-23, and iv) the Hb binding site on band 3 lies proximal to binding sites for glycolytic enzymes, band 4.1 and ankyrin, suggesting possible mechanisms through which multifarious erythrocyte properties might be regulated by the oxygenation state of the cell. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: I. A. Lewis, M. E. Campanella, J. L. Markley, and P. S. Low Role of band 3 in regulating metabolic flux of red blood cells PNAS, November 3, 2009; 106(44): 18515 - 18520. [Abstract] [Full Text] [PDF] S. C. Rogers, A. Said, D. Corcuera, D. McLaughlin, P. Kell, and A. Doctor Hypoxia limits antioxidant capacity in red blood cells by altering glycolytic pathway dominance FASEB J, September 1, 2009; 23(9): 3159 - 3170. [Abstract] [Full Text] [PDF] S. L. Alper Molecular physiology and genetics of Na+-independent SLC4 anion exchangers J. Exp. Biol., June 1, 2009; 212(11): 1672 - 1683. [Abstract] [Full Text] [PDF] M. E. Campanella, H. Chu, N. J. Wandersee, L. L. Peters, N. Mohandas, D. M. Gilligan, and P. S. Low Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice Blood, November 1, 2008; 112(9): 3900 - 3906. [Abstract] [Full Text] [PDF]

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