Mutual effects of proton and sodium chloride on oxygenation of liganded human hemoglobin: Oxygen affinities of the α and β subunits

FEBS Journal

Volumn 272, Issue 23, 2005, Pages 6109-6119

  Lepeshkevich, Sergei V ^a   Dzhagarov, Boris M ^a  

^a B I STEPANOV INSTITUTE OF PHYSICS   (Belarus)

Author keywords

and subunits; Affinity; Human hemoglobin; Molecular oxygen; Sodium chloride

Indexed keywords

HEMOGLOBIN; HEMOGLOBIN A; OXYGEN; PROTON; SODIUM CHLORIDE;

ALPHA CHAIN; ARTICLE; BETA CHAIN; BLOOD OXYGENATION; CONTROLLED STUDY; DISSOCIATION CONSTANT; HUMAN; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; OXYGEN AFFINITY; OXYGEN DISSOCIATION CURVE; OXYGEN TRANSPORT; PH MEASUREMENT; PHOTOLYSIS; PRIORITY JOURNAL; PROTON TRANSPORT; SODIUM TRANSPORT;

DIMERIZATION; HEMOGLOBIN A; HUMANS; HYDROGEN-ION CONCENTRATION; LIGANDS; LIGHT; OXIDATION-REDUCTION; OXYGEN; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PROTONS; SODIUM CHLORIDE; SPECTRUM ANALYSIS;

EID: 28244449040     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.05008.x     Document Type: Article

References (49)

1. Perutz MF, Wilkinson AJ, Paoli M & Dodson GG (1998) The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annu Rev Biophys Biomol Struct 27, 1-34.
2. Antonini E & Brunori M (1971) Hemoglobin and Myoglobin in Their Reaction with Ligands. North-Holland, Amsterdam.
3. Ackers GK, Doyle ML, Myers D & Daugherty MA (1992) Molecular code for cooperativity in hemoglobin. Science 255, 54-63.
4. Parkhust LJ (1979) Hemoglobin and myoglobin ligand kinetics. Annu Rev Phys Chem 30, 503-546.
5. Henry ER, Bettati S, Hofrichter J & Eaton WA (2002) A tertiary two-state allosteric model for hemoglobin. Biophys Chem 98, 149-164.
6. 2 affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors. J Biol Chem 277, 34508-34520.
7. Viappiani C, Bettati S, Bruno S, Ronda L, Abbruzzetti S, Mozzarelli A & Eaton WA (2004) New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels. Proc Natl Acad Sci USA 101, 14414-14419.
8. Gibson QH (1959) The photochemical formation of a quickly reacting form of haemoglobin. Biochem J 71, 293-303.
9. Austin RH, Beeson KW, Eisenstein L, Frauenfelder H & Gunsalus IC (1975) Dynamics of ligand binding to myoglobin. Biochemistry 14, 5355-5373.
10. Mathews AJ, Rohlfs RJ, Olson JS, Tame J, Renaud J-P & Nagai K (1989) The effects of E7 and E11 mutation on the kinetics of ligand binding to R state human hemoglobin. J Biol Chem 264, 16573-16583.
11. Murray LP, Hofrichter J, Henry ER & Eaton WA (1988) Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbon monoxyhemoglobin. Biophys Chem 29, 63-76.
12. Peterson ES, Shinder R, Khan I, Juczszak L, Wang J, Manjula B, Acharya SA, Bonaventura C & Friedman JM (2004) Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways. Biochemistry 43, 4832-4843.
13. 2 and CO binding to the α and β subunits within the R and T states of human hemoglobin. J Biol Chem 273, 23150-23159.
14. Philo JS & Lary JW (1990) Kinetic investigations of the quaternary enhancement effect and α/β differences in binding the last oxygen to hemoglobin tetramers and dimers. J Biol Chem 265, 139-143.
15. Lepeshkevich SV, Konovalova NV & Dzhagarov BM (2003) Laser kinetic studies of bimolecular oxygenation reaction of α and β subunits within the R state of human hemoglobin. Biokhimia (Moscow) 68, 676-685.
16. Lepeshkevich SV, Karpiuk J, Sazanovich IV & Dzhagarov BM (2004) A kinetic description of dioxygen motion within alpha- and beta-subunits of human hemoglobin in the R-state: geminate and bimolecular stages of the oxygenation reaction. Biochemistry 43, 1675-1684.
17. Dzhagarov BM & Lepeshkevich SV (2004) Kinetic studies of differences between α- and β-chains of human hemoglobin: an approach for determination of the chain affinity to oxygen. Chem Phys Lett 390, 59-64.
18. Lepeshkevich SV, Konovalova NV, Stepuro II & Dzhagarov BM (2005) Laser kinetic studies of bimolecular oxygenation reaction of alpha- and beta-subunits within pyridoxal 5′-phosphate derivatives of human hemoglobin. J Mol Struct 735-736C, 307-313.
19. Gibson QH & Roughton FJW (1955) The kinetics of dissociation of the first oxygen molecule from fully saturated oxyhaemoglobin in sheep blood solutions. Proc R Soc. Series B 143, 310-334.
20. MacQuarrie R & Gibson QH (1972) Ligand binding and release of an analogue of 2,3-diphosphoglycerate from human hemoglobin. J Biol Chem 247, 5686-5694.
21. Kwiatkowski LD & Noble RW (1982) The contribution of histidine (HC3) (146β) to the R state Bohr effect of human hemoglobin. J Biol Chem 257, 8891-8895.
22. 3. Biophys (Russian) 41, 607-612.
23. Imai K & Yonetani T (1975) pH dependence of the Adair constants of human hemoglobin. Nonuniform contribution of successive oxygen binding to the alkaline Bohr effect. J Biol Chem 250, 2227-2231.
24. Sawicki CA & Gibson QH (1976) Quaternary changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin. J Biol Chem 251, 1533-1542.
25. Gibson QH (1999) Kinetics of oxygen binding to hemoglobin A. Biochemistry 38, 5191-5199.
26. Dzhagarov BM, Galievsky VA, Kruk NN & Yakutovich MD (1999) Photodissociation of oxygenated forms of the native hemoglobin HbA and its isolated α- and β-subunits and kinetics of molecular oxygen rebinding. Dokl Biophys (translation of Dokl Akad Nauk) 366, 38-41.
27. Guidotti G (1967) Studies on the chemistry of hemoglobin. II. The effect of salts on the dissociation of hemoglobin into subunits. J Biol Chem 242, 3685-3693.
28. Kirshner AG & Tanford C (1964) The dissociation of hemoglobin by inorganic salts. Biochemistry 3, 291-296.
29. Atha DH & Riggs A (1976) Tetramer-dimer dissociation in hemoglobin and the Bohr effect. J Biol Chem 251, 5537-5543.
30. Ip SHC & Ackers GK (1977) Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobin. J Biol Chem 252, 82-87.
31. 2 binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect. Biophys Chem 64, 271-287.
32. Kellett GL & Schachman HK (1971) Dissociation of hemoglobin into subunits. Monomer formation and the influence of ligands. J Mol Biol 59, 387-399.
33. Kellett GL (1971) Dissociation of hemoglobin into subunits. Ligand-linked dissociation at neutral pH. J Mol Biol 59, 401-424.
34. Eaton WA (1980) The relationship between coding sequences and function in haemoglobin. Nature 284, 183-185.
35. Chiancone E, Norne JE, Forsén S, Antonini E & Wyman J (1972) Nuclear magnetic resonance quadrupole relaxation studies of chloride binding to human oxy- and deoxyhaemoglobin. J Mol Biol 70, 675-688.
36. O'Donnell S, Mandaro R, Schuster TM & Arnone A (1979) X-Ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1α. J Biol Chem 254, 12204-12208.
37. 35Cl binding to human oxy- and carbon monoxyhaemoglobin. J Mol Biol 73, 251-259.
38. Colombo MF, Rau DC & Parsegian VA (1992) Protein solvation in allosteric regulation: a water effect on hemoglobin. Science 256, 655-659.
39. Salvay AG, Grigera JR & Colombo MF (2003) The role of hydration on the mechanism of allosteric regulation: in situ measurements of the oxygen-linked kinetics of water binding to hemoglobin. Biophys J 84, 564-570.
40. Silva MM, Rogers PH & Arnone A (1992) A third quaternary structure of human hemoglobin A at 1.7-Å resolution. J Biol Chem 267, 17248-17256.
41. Shaanan B (1983) Structure of human oxyhaemoglobin at 2.1 Å resolution. J Mol Biol 171, 31-59.
42. Mueser TC, Rogers PH & Arnone A (2000) Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin. Biochemistry 39, 15353-15364.
43. Lukin JA, Kontaxis G, Simplaceanu V, Yuan Y, Bax A & Ho C (2003) Quaternary structure of hemoglobin in solution. Proc Nat Acad Sci USA 100, 517-520.
44. Safo MK & Abraham DJ (2005) The enigma of the liganded hemoglobin end state: a novel quaternary structure of human carbon monoxyhemoglobin. Biochemistry 44, 8347-8359.
45. Lindstrom TR & Ho C (1973) Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin. Biochemistry 12, 134-139.
46. Ho C (1992) Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially liganted intermediates. Adv Protein Chem 43, 153-311.
47. Bucci E & Fronticelli C (1965) A new method for the preparation of α and β subunits of human hemoglobin. J Biol Chem 240, 551-552.
48. Haire RN & Hedlund BE (1977) Thermodynamic aspects of the linkage between binding of chloride and oxygen to human hemoglobin. Proc Natl Acad Sci USA 74, 4135-4138.
49. Griva ZI, Kotz VA & Tomarchenko SL, eds. (1967) Handbook of Chemistry IV. Khimia, Leningrad.