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Related Experiment Videos

Metastable intermediates in myoglobin at low pH.

S Han1, D L Rousseau, G Giacometti

  • 1AT&T Bell Laboratories, Murray Hill, NJ 07974.

Proceedings of the National Academy of Sciences of the United States of America
|January 1, 1990
PubMed
Summary
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Ligand-free myoglobin

Area of Science:

  • Biochemistry
  • Spectroscopy
  • Protein dynamics

Background:

  • Myoglobin's structure and function are pH-dependent.
  • Understanding hemoprotein dynamics at low pH is crucial.

Purpose of the Study:

  • To investigate structural changes in myoglobin at low pH.
  • To elucidate the role of the iron-histidine bond in myoglobin function.

Main Methods:

  • Resonance Raman spectroscopy
  • Optical absorption spectroscopy
  • Continuous-flow/rapid-mixing techniques

Main Results:

  • At low pH, the iron-histidine bond in ligand-free myoglobin breaks, replaced by a weak-field ligand.
  • CO-bound myoglobin shows an intact iron-histidine bond and an open distal pocket at low pH.

Related Experiment Videos

  • Protein constraints on the heme group relax in CO-bound myoglobin at low pH.

    • Conclusions:

    • Low pH induces distinct structural changes in myoglobin.
    • These findings support and refine previous conclusions on hemoprotein kinetics at low pH.