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Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted).

Fronticelli C, Pechik I, Brinigar WS, Kowalczyk J, Gilliland GL
J Biol Chem 269 23965-9 (1994)
Cited: 22 times
EuropePMC logo PMID: 7929044

Abstract

A mutant human hemoglobin, beta (V1M+H2 delta), has been constructed. Analysis of the oxygen binding curves obtained at pH 8.3, where the Bohr effect is inoperative, indicates that this mutation results in an additional stabilization of the T-state conformation by 0.9 kcal/mol. The crystal structure of deoxy-beta (V1M+H2 delta) has been determined to 2.2-A resolution and compared with the deoxy structure of human hemoglobin at the same resolution. In human hemoglobin, a sulfate anion is anchored to the beta-chains by a complex network of H-bonds and electrostatic interactions with the amino terminus and Lys beta 82. In the mutant hemoglobin, the shortening of the amino-terminal region of the A helix by 1 residue results in the formation of an intrachain electrostatic interaction between the amino-terminal amino and Asp beta 79. This eliminates the sulfate binding site, and the sulfate is replaced by two water molecules. At variance with human hemoglobin, the alkaline Bohr effect for beta (V1M+H2 delta) is not sensitive to the presence of Cl-. This indicates that the sulfate binding site in human hemoglobin also serves as a Cl- binding site, and that the amino-terminal Val beta 1 is essential for oxygen-linked Cl- binding to hemoglobin as well as the Cl(-)-dependent Bohr effect. Analysis of the oxygen binding curves indicates that the oxygen-linked Cl- ions are released upon binding of the first oxygen molecule.

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Reviews citing this publication (3)

  1. Hemoglobin: Structure, Function and Allostery. Ahmed MH, Ghatge MS, Safo MK. Subcell Biochem 94 345-382 (2020)
  2. New insights into the proton-dependent oxygen affinity of Root effect haemoglobins. Bonaventura C, Crumbliss AL, Weber RE. Acta Physiol Scand 182 245-258 (2004)
  3. Remote contributions to subunit interactions: lessons from adult and fetal hemoglobins. Manning JM, Dumoulin A, Manning LR, Chen W, Padovan JC, Chait BT, Popowicz A. Trends Biochem Sci 24 211-212 (1999)

Articles citing this publication (18)

  1. Novel mechanism for high-altitude adaptation in hemoglobin of the Andean frog Telmatobius peruvianus. Weber RE, Ostojic H, Fago A, Dewilde S, Van Hauwaert ML, Moens L, Monge C. Am J Physiol Regul Integr Comp Physiol 283 R1052-60 (2002)
  2. Allosteric modulation by tertiary structure in mammalian hemoglobins. Introduction of the functional characteristics of bovine hemoglobin into human hemoglobin by five amino acid substitutions. Fronticelli C, Sanna MT, Perez-Alvarado GC, Karavitis M, Lu AL, Brinigar WS. J Biol Chem 270 30588-30592 (1995)
  3. Glycated human hemoglobin (HbA1c): functional characteristics and molecular modeling studies. De Rosa MC, Sanna MT, Messana I, Castagnola M, Galtieri A, Tellone E, Scatena R, Botta B, Botta M, Giardina B. Biophys Chem 72 323-335 (1998)
  4. High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector. Safo MK, Moure CM, Burnett JC, Joshi GS, Abraham DJ. Protein Sci 10 951-957 (2001)
  5. The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity. Fago A, Carratore V, di Prisco G, Feuerlein RJ, Sottrup-Jensen L, Weber RE. J Biol Chem 270 18897-18902 (1995)
  6. Cysteines beta93 and beta112 as probes of conformational and functional events at the human hemoglobin subunit interfaces. Vásquez GB, Karavitis M, Ji X, Pechik I, Brinigar WS, Gilliland GL, Fronticelli C. Biophys J 76 88-97 (1999)
  7. From the Arctic to fetal life: physiological importance and structural basis of an 'additional' chloride-binding site in haemoglobin. De Rosa MC, Castagnola M, Bertonati C, Galtieri A, Giardina B. Biochem J 380 889-896 (2004)
  8. Enthalpic partitioning of the reduced temperature sensitivity of O2 binding in bovine hemoglobin. Weber RE, Fago A, Campbell KL. Comp Biochem Physiol A Mol Integr Physiol 176 20-25 (2014)
  9. Introduction of a new regulatory mechanism into human hemoglobin. Fronticelli C, Bobofchak KM, Karavitis M, Sanna MT, Brinigar WS. Biophys Chem 98 115-126 (2002)
  10. Alpha-subunit oxidation in T-state crystals of a sebacyl cross-linked human hemoglobin with unusual autoxidation properties. Ji X, Karavitis M, Razynska A, Kwansa H, Vásquez G, Fronticelli C, Bucci E, Gilliland GL. Biophys Chem 70 21-34 (1998)
  11. Dynamic properties of some beta-chain mutant hemoglobins. Militello V, Cupane A, Leone M, Brinigar WS, Lu AL, Fronticelli C. Proteins 22 12-19 (1995)
  12. Enthalpic consequences of reduced chloride binding in Andean frog (Telmatobius peruvianus) hemoglobin. Weber RE. J Comp Physiol B 184 613-621 (2014)
  13. Importance of helices A and H in oxygen binding differences between bovine and human hemoglobins. Baudin-Creuza V, Vasseur-Godbillon C, Kister J, Domingues E, Poyart C, Marden M, Pagnier J. Hemoglobin 26 373-384 (2002)
  14. Conformation of the sebacyl beta1Lys82-beta2Lys82 crosslink in T-state human hemoglobin. Ji X, Braxenthaler M, Moult J, Fronticelli C, Bucci E, Gilliland GL. Proteins 30 309-320 (1998)
  15. Structure of deoxyhemoglobin: ionizable groups and polyethylene glycol. Saroff HA. Proteins 50 329-340 (2003)
  16. Characterization of the hemoglobins of the adult brushtailed possum, Trichosurus vulpecula (Kerr) reveals non-genetic heterogeneity. Henty K, Wells RM, Brittain T. Comp Biochem Physiol A Mol Integr Physiol 148 498-503 (2007)
  17. Different functional modulation by heterotropic ligands (2,3-diphosphoglycerate and chlorides) of the two haemoglobins from fallow-deer (Dama dama). Angeletti M, Pucciarelli S, Priori AM, Canofeni S, Barra D, Fioretti E, Coletta M. Eur J Biochem 268 603-611 (2001)
  18. Macromolecular Crystallography and Structural Biology Databases at NIST. Gilliland GL. J Res Natl Inst Stand Technol 106 1155-1173 (2001)


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