Site mutations disrupt inter-helical H-bonds (α14W-α67T and β15W-β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation

Biophysical Chemistry

Volumn 100, Issue 1-3, 2002, Pages 131-142

  Tsai, Ching Hsuan ^a   Simplaceanu, Virgil ^a   Ho, Nancy T ^a   Shen, Tong Jian ^a   Wang, Daojing ^b   Spiro, Thomas G ^b   Ho, Chien ^a  

^a CARNEGIE MELLON UNIVERSITY   (United States)

^b PRINCETON UNIVERSITY   (United States)

Author keywords

Hemoglobin; Inter helical H bonds; Site mutations

Indexed keywords

BUFFER; HEMOGLOBIN A; HEMOGLOBIN ALPHA CHAIN; HEMOGLOBIN BETA CHAIN; HYDROGEN; MUTANT PROTEIN; RECOMBINANT HEMOGLOBIN; SODIUM DIHYDROGEN PHOSPHATE;

ADULT; ALLOSTERISM; ARTICLE; BINDING AFFINITY; BINDING KINETICS; CONTROLLED STUDY; HEMOGLOBIN SYNTHESIS; HUMAN; HYDROGEN BOND; MUTATION; OXYGEN AFFINITY; OXYGENATION; PH; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 0037438352     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00274-0     Document Type: Article

References (42)

1. Perutz M.F. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:1970;726-739.
2. Fermi G., Perutz M.F., Shaanan B., Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175:1984;159-174.
3. Baldwin J.M. The structure of human carbonmonoxy haemoglobin at 2.7 Å resolution. J. Mol. Biol. 136:1980;103-128.
4. Shaanan B. Structure of human oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 171:1983;31-59.
5. Ho C., Lukin J.A. Haemoglobin: cooperativity in protein-ligand interaction. Encyclopedia of Life Sciences. 2000;Macmillan, London, (http://www.els.net).
6. Rodgers K.R., Spiro T.G. Nanosecond dynamics of the R→T transition in hemoglobin: ultraviolet Raman studies. Science. 265:1994;1697-1699.
7. Jayaraman V., Rodgers K.R., Mukerji I., Spiro T.G. Hemoglobin allostery: resonance Raman spectroscopy of kinetic intermediates. Science. 269:1995;1843-1848.
8. Hu X., Rodgers K.R., Mukerji I., Spiro T.G. New light on allostery: dynamic resonance Raman spectroscopy of hemoglobin Kempsey. Biochemistry. 38:1999;3462-3467.
9. Juszczak I.J., Friedman J.M. UV resonance Raman Spectra of ligand binding intermediates of sol-gel encapsulated hemoglobin. J. Biol. Chem. 274:1999;30357-30360.
10. Wang D., Zhao X., Shen T.-J., Ho C., Spiro T.G. Role of interhelical H-Bonds [Wα14-Tα67 and Wβ15-Sβ72) in the hemoglobin allosteric reaction path evaluated by UV resonance Raman spectroscopy of site-mutants. J. Am. Chem. Soc. 121:1999;11197-11203.
11. Ho C. Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates. Adv. Protein Chem. 42:1992;153-312.
12. Llinas M., Klein M.P., Neilands J.B. Solution conformation of the ferrichromes. A comparative proton magnetic resonance study of glycine- and serine-containing ferrichromes. J. Mol. Biol. 68:1972;265-284.
13. Fung L.W.-M., Ho C. A proton nuclear magnetic resonance study of the quaternary structure of human homoglobins in water. Biochemistry. 14:1975;2526-2535.
14. Viggiano G., Ho C. Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin. Proc. Natl. Acad. Sci. USA. 76:1979;3673-3677.
15. Wagner G., Pardi A., Wuthrich K. Hydrogen-bond length and H-1-NMR chemical-shifts in proteins. J. Am. Chem. Soc. 105:1983;5948-5949.
16. Redfield A.G., Papastratos M.Z. NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21. Biochemistry. 29:1990;3509-3514.
17. 2 interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (βL105W). Biochemistry. 39:2000;13708-13718.
18. Lukin J.A., Simplaceanu V., Zou M., Ho N.T., Ho C. NMR reveals hydrogen bonds between oxygen and distal histidines in oxyhemoglobin. Proc. Natl. Acad. Sci. USA. 97:2000;10354-10358.
19. Nocek J.M., Huang K., Hoffman B.M. Extension of transverse relaxation-optimized spectroscopy techniques to allosteric proteins: CO- and paramagnetic fluoromet-hemoglobin [beta (15N-valine)]. Proc. Natl. Acad. Sci. USA. 97:2000;2538-2543.
20. Simplaceanu V., Lukin J.A., Fang T.-Y., Zou M., Ho N.T., Ho C. Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin. Biophys. J. 79:2000;1146-1154.
21. Shen T.-J., Ho N.T., Simplaceanu V., et al. Production of unmodified human adult hemoglobin in Escherichia coli. Proc. Natl. Acad. Sci. USA. 90:1993;8108-8112.
22. Shen T.-J., Ho N.T., Zou M., et al. Production of human normal adult and fetal hemoglobins in Escherichia coli. Protein Eng. 10:1997;1085-1097.
23. 2 subunit interfaces in the cooperative oxygenation process. Biochemistry. 38:1999;8751-8761.
24. Hayashi A., Suzuki T., Shin M. Enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers. Biochim. Biophys. Acta. 310:1973;309-316.
25. Plateau P., Guéron M. Exchangeable proton NMR without base-line distortion, using new strong-pulse sequences. J. Am. Chem. Soc. 104:1982;7310-7311.
26. Kim H.-W., Shen T.-J., Sun D.P., et al. Restoring allosterism with compensatory mutations in hemoglobin. Proc. Natl. Acad. Sci. USA. 91:1994;11547-11551.
27. Kim H.-W., Shen T.-J., Sun D.P., Ho N.T., Madrid M., Ho C. A novel low oxygen affinity recombinant hemoglobin (α96val→Trp): switching quaternary structure without changing the ligation state. J. Mol. Biol. 248:1995;867-882.
28. Kim H.-W., Shen T.-J., Ho N.T., Zou M., Tam M.F., Ho C. Contributions of asparagine at α97 to the cooperative oxygenation process of hemoglobin. Biochemistry. 35:1996;6620-6627.
29. Ho C., Willis B.F., Shen T.-J., et al. Roles of α114 and β87 amino acid residues in the polymerization of hemoglobin S: implications for gene therapy. J. Mol. Biol. 263:1996;475-485.
30. Ho C., Sun D.P., Shen T.-J., et al. Recombinant hemoglobins with low oxygen affinity and high cooperativity. Tsuchida E. Present and Future Perspectives of Blood Substitutes. 1998;281-296 Elsevier Science SA, Lausanne, Switzerland.
31. Barrick D., Ho N.T., Simplaceanu V., Dahlquist F.W., Ho C. A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin. Nat. Struct. Biol. 4:1997;78-83.
32. Russu I.M., Ho N.T., Ho C. A proton nuclear overhauser effect investigation of the subunit interfaces in human normal adult hemoglobin. Biochim. Biophys. Acta. 914:1987;40-48.
33. 2 subunit interfaces. Biochemistry. 41:2002;5644-5655.
34. Lindstrom T.R., Norén I.B.E., Charache S., Lehmann H., Ho C. Nuclear magnetic resonance studies of hemoglobins. VII. Tertiary structure around ligand binding site in carbonmonoxyhemoglobin. Biochemistry. 11:1972;1677-1681.
35. Dalvit C., Ho C. Proton nuclear overhauser effect investigation of the heme pockets in ligated hemoglobin: conformational differences between oxy and carbonmonoxy forms. Biochemistry. 24:1985;3398-3407.
36. Sun D.P., Zou M., Ho N.T., Ho C. Contribution of surface histidyl residues in the alpha-chain to the Bohr effect of human normal adult hemoglobin: roles of global electrostatic effects. Biochemistry. 36:1997;6663-6673.
37. Ishimori K., Imai K., Miyazaki G., et al. Site-directed mutagenesis in hemoglobin: functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37 beta and 145 beta mutations. Biochemistry. 31:1992;3256-3264.
38. Yuan Y., Simplaceanu V., Lukin J.A., Ho C. NMR investigation of dynamics of tryptophan side-chains in hemoglobins. J. Mol. Biol. 321:2002;863-878.
39. Silva M.M., Rogers P.H., Arnone A. A third quaternary structure of human hemoglobin A at 1.7-Å resolution. J. Biol. Chem. 267:1992;17248-17256.
40. Dickerson R.E., Geis I. Hemoglobin: Structure, Function, Evolution, and Pathology. 1983;Benjamin/Cummings, Menlo Park.
41. Huisman T.H.J., Carver M.F.H., Efemov G.D. A Syllabus of Human Hemoglobin Variants, 2nd ed. 1998;The Sickle Cell Anemia Foundation, Augusta, GA, USA.
42. Loria J.P., Rance M., Palmer A.G. A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR. 15:1999;151-155.