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Related Experiment Videos

Oxymyohemerythrin: discriminating between O2 release and autoxidation.

C R Lloyd1, G M Raner, A Moser

  • 1Department of Chemistry, University of Utah, Salt Lake City 84112, USA.

Journal of Inorganic Biochemistry
|November 7, 2000
PubMed
Summary

Myohemerythrin (Mhr), an oxygen carrier, undergoes distinct reactions including O2 release and autoxidation. Environmental factors significantly influence these processes, with specific mutations like L103V/N dramatically accelerating autoxidation.

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Biophysical Chemistry

Background:

  • Myohemerythrin (Mhr) is a non-heme iron O2 carrier found in marine worms.
  • OxyMhr can release O2 or undergo autoxidation, producing hydrogen peroxide and metMhr.
  • Anions can promote Mhr autoxidation.

Purpose of the Study:

  • To investigate environmental effects on Mhr's O2 release and autoxidation reactions.
  • To compare kinetic parameters of O2 release versus autoxidation.
  • To explore the role of specific mutations and anions in Mhr reactivity.

Main Methods:

  • Utilized recombinant Themiste zostericola Mhrs.
  • Measured kinetic parameters (deltaV‡, deltaH‡, deltaS‡) for O2 release and autoxidation.
  • Investigated reactions with and without sodium azide, and studied L103V/N mutants.

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Main Results:

  • O2 release and autoxidation exhibit distinct thermodynamic and kinetic parameters.
  • Autoxidation is significantly accelerated by sodium azide.
  • L103V and L103N oxyMhr mutants autoxidize 10^3-10^5 times faster than wild-type Mhr.

Conclusions:

  • Leucine-103 is crucial for stabilizing bound dioxygen, potentially acting as a protein gate.
  • The rate-limiting steps for Mhr autoxidation and anation are not solely ligand binding.
  • Environmental factors and protein structure play key roles in Mhr's oxygen-binding and reaction dynamics.