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Solution structure and dynamics of human hemoglobin in the carbonmonoxy form.

Fan JS, Zheng Y, Choy WY, Simplaceanu V, Ho NT, Ho C, Yang D
Biochemistry 52 5809-20 (2013)
Cited: 15 times
EuropePMC logo PMID: 23901897

Abstract

The solution structure of human adult carbonmonoxy hemoglobin (HbCO A) was refined using stereospecifically assigned methyl groups and residual dipolar couplings based on our previous nuclear magnetic resonance structure. The tertiary structures of individual chains were found to be very similar to the X-ray structures, while the quaternary structures in solution at low salt concentrations resembled the X-ray R structure more than the R2 structure. On the basis of chemical shift perturbation by inositol hexaphosphate (IHP) titration and docking, we identified five possible IHP binding sites in HbCO A. Amide-water proton exchange experiments demonstrated that αThr38 located in the α1β2 interface and several loop regions in both α- and β-chains were dynamic on the subsecond time scale. Side chain methyl dynamics revealed that methyl groups in the α1β2 interface were dynamic, but those in the α1β1 interface were quite rigid on the nanosecond to picosecond and millisecond to microsecond time scales. All the data strongly suggest a dynamic α1β2 interface that allows conformational changes among different forms (like T, R, and R2) easily in solution. Binding of IHP to HbCO A induced small structural and dynamic changes in the α1β2 interface and the regions around the hemes but did not increase the conformational entropy of HbCO A. The binding also caused conformational changes on the millisecond time scale, very likely arising from the relative motion of the α1β1 dimer with respect to the α2β2 dimer. Heterotropic effectors like IHP may change the oxygen affinity of Hb through modulating the relative motion of the two dimers and then further altering the structure of heme binding regions.

Reviews - 2m6z mentioned but not cited (2)

  1. New look at hemoglobin allostery. Yuan Y, Tam MF, Simplaceanu V, Ho C. Chem Rev 115 1702-1724 (2015)
  2. Dietary Heme-Containing Proteins: Structures, Applications, and Challenges. Xing Y, Gao S, Zhang X, Zang J. Foods 11 3594 (2022)

Articles - 2m6z mentioned but not cited (7)

  1. Strain analysis of protein structures and low dimensionality of mechanical allosteric couplings. Mitchell MR, Tlusty T, Leibler S. Proc Natl Acad Sci U S A 113 E5847-E5855 (2016)
  2. Solution structure and dynamics of human hemoglobin in the carbonmonoxy form. Fan JS, Zheng Y, Choy WY, Simplaceanu V, Ho NT, Ho C, Yang D. Biochemistry 52 5809-5820 (2013)
  3. Dynamics based clustering of globin family members. Tobi D. PLoS One 13 e0208465 (2018)
  4. New Insights into Hemopexin-Binding to Hemin and Hemoglobin. Lechuga GC, Napoleão-Pêgo P, Morel CM, Provance DW, De-Simone SG. Int J Mol Sci 23 3789 (2022)
  5. Understanding the roles of intrinsic disorder in subunits of hemoglobin and the disease process of sickle cell anemia. Fitzsimmons R, Amin N, Uversky VN. Intrinsically Disord Proteins 4 e1248273 (2016)
  6. Coarse-grain simulations on NMR conformational ensembles highlight functional residues in proteins. Sacquin-Mora S. J R Soc Interface 16 20190075 (2019)
  7. Identification of Blood Transport Proteins to Carry Temoporfin: A Domino Approach from Virtual Screening to Synthesis and In Vitro PDT Testing. Marconi A, Giugliano G, Di Giosia M, Marforio TD, Trivini M, Turrini E, Fimognari C, Zerbetto F, Mattioli EJ, Calvaresi M. Pharmaceutics 15 919 (2023)


Reviews citing this publication (2)

  1. Hemoglobin: Structure, Function and Allostery. Ahmed MH, Ghatge MS, Safo MK. Subcell Biochem 94 345-382 (2020)
  2. Carbon Monoxide Signaling: Examining Its Engagement with Various Molecular Targets in the Context of Binding Affinity, Concentration, and Biologic Response. Yuan Z, De La Cruz LK, Yang X, Wang B. Pharmacol Rev 74 823-873 (2022)

Articles citing this publication (4)

  1. Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study. Jones EM, Monza E, Balakrishnan G, Blouin GC, Mak PJ, Zhu Q, Kincaid JR, Guallar V, Spiro TG. J Am Chem Soc 136 10325-10339 (2014)
  2. An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 Tetramer. Nagatomo S, Nagai Y, Aki Y, Sakurai H, Imai K, Mizusawa N, Ogura T, Kitagawa T, Nagai M. PLoS One 10 e0135080 (2015)
  3. Dynamics of Quaternary Structure Transitions in R-State Carbonmonoxyhemoglobin Unveiled in Time-Resolved X-ray Scattering Patterns Following a Temperature Jump. Cho HS, Schotte F, Stadnytskyi V, DiChiara A, Henning R, Anfinrud P. J Phys Chem B 122 11488-11496 (2018)
  4. Modulation of hemoglobin dynamics by an allosteric effector. Lal J, Maccarini M, Fouquet P, Ho NT, Ho C, Makowski L. Protein Sci 26 505-514 (2017)


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