Hemoglobin Oxygenation Dynamics on Picosecond Time Scale

  • B. M. Dzhagarov
  • N. N. Kruk
  • S. A. Tikhomirov
  • V. A. Galievsky
Chapter

Abstract

The binding of ligands by proteins is a fundamental biological process. The sequential binding (oxygenation) of four oxygen molecules to the tetrameric protein hemoglobin is a basic reaction for the study of a cooperative ligand binding and allosteric interactions in protein and enzymes1–4. The affinity of Hb to O2 rises with the ligand saturation and tuned by different heterotropic effectors. In particular the proton concentration determines the hemoglobin affinity to O2 (Bohr effect) and regulates the CO2/O2 exchange by Hb in the tissues1–4. Every subunit of tetrameric hemoglobin molecule has a Fe(II)-protoporphyrin-IX (heme) as an active site, which is situated inside the folded polypeptide chain. Motion of the unbound oxygen molecule in the interior of the globin matrix is mediated by the protein moiety. The laser time-resolved spectroscopy provides a powerful method for the study of the kinetics parameters of the oxygenation because the photoexcitation leads to the very rapid dissociation of O2 5. The oxy-Hb photodissociation triggers events which can be followed by time-resolved spectroscopy monitoring of the transient optical spectrum5–19. The principal point of such experiments is a study of the direct oxygen re-binding with the paternal heme from the bulk protein. This phenomenon is known as a geminate rebinding (GR) and provides the important information about the protein function and structure. This paper is devoted to the investigation of the protein control of the ligand geminate rebinding under the different pH values. The main goal of these studies was to measure the primary quantum yield of the oxy-Hb photodissociation and to elucidate the dynamics of the oxygen motion in the interior of protein. Earlier we presented the results of the measurements of the efficiences and rates of the geminate and nongeminate rebinding processes in the large range of the pH values19, 20. Now we present the refined kinetic data obtained for the geminate stages of the ligand rebinding and discuss the protein control of the GR.

Keywords

Oxygen Molecule Nauk USSR Heme Pocket Apparent Quantum Yield Bohr Effect 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • B. M. Dzhagarov
    • 1
  • N. N. Kruk
    • 1
  • S. A. Tikhomirov
    • 1
  • V. A. Galievsky
    • 1
  1. 1.Institute of Molecular and Atomic PhysicsBelarus Academy of SciencesMinskBelarus

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