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Fe-heme conformations in ferric myoglobin

S Della Longa1, S Pin, R Cortès

  • 1Dept. Medicina Sperimentale and INFM, Università dell'Aquila, I-67100 L'Aquila and Ist. Naz. Fisica Materia (INFM), Italy. dellalongo@vaxaq

Biophysical Journal
|November 25, 1998
PubMed
Summary

This study reveals three distinct ferric myoglobin conformations using X-ray absorption near-edge structure (XANES) spectroscopy. These conformations are linked to pH changes and involve shifts in the iron-heme structure and spin states.

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Area of Science:

  • Biophysics
  • Biochemistry
  • Spectroscopy

Background:

  • Myoglobin is a vital protein for oxygen transport.
  • Understanding ferric myoglobin's structure is key to its function.
  • pH and temperature influence protein conformation and spin states.

Purpose of the Study:

  • To investigate the structural and spin state changes of ferric myoglobin across a pH range.
  • To characterize the Fe-heme conformations under varying conditions.
  • To elucidate the relationship between pH, temperature, and myoglobin's electronic structure.

Main Methods:

  • X-ray absorption near-edge structure (XANES) spectroscopy was employed.
  • Spectra were collected as a function of pH (5.3–11.3) and temperature (20–293 K) at pH 11.3.

Related Experiment Videos

  • Spin-resolved multiple scattering simulations were used for data fitting and structural assignment.

    • Main Results:

    • Three distinct Fe-heme conformations were identified.
    • At low pH, aquomet-myoglobin (Mb+OH2) in a high-spin state was observed.
    • At pH 11.3, hydroxymet-myoglobin (Mb+OH-) exhibited two conformations in thermal equilibrium: high-spin and low-spin states.
    • Transitions involved changes in the Fe coordination sphere, movement towards the heme plane, and increased axial asymmetry.

    Conclusions:

    • The study successfully characterized three Fe-heme conformations of ferric myoglobin.
    • pH-dependent transitions between aquomet- and hydroxymet-myoglobin involve significant structural rearrangements.
    • The spin transition in hydroxymet-myoglobin is coupled with changes in the Fe coordination sphere and axial asymmetry.