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Evolving the [myoglobin, cytochrome b(5)] complex from dynamic toward simple docking: charging the electron transfer

Ethan N Trana1, Judith M Nocek, Amanda K Knutson

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We engineered Zn-substituted myoglobin (Mb) variants to study electron transfer (ET) with cytochrome b(5). Modifying protein charges significantly altered binding affinity and ET rates, revealing a simple electrostatic dependence.

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Electron Transfer Dynamics

Background:

  • Electron transfer (ET) between proteins is crucial for biological processes.
  • Myoglobin (Mb) and cytochrome b(5) (b(5)) are key proteins involved in electron transport.
  • Understanding the factors governing protein-protein interactions and ET rates is essential.

Purpose of the Study:

  • To investigate the impact of electrostatic interactions on electron transfer between myoglobin and cytochrome b(5).
  • To engineer myoglobin variants with altered charge distributions near the heme edge.
  • To quantify the relationship between binding affinity, charge interactions, and electron transfer kinetics.

Main Methods:

  • Utilized site-directed mutagenesis to introduce charge-reversal mutations (D/E to K) in myoglobin variants.
  • Neutralization of heme propionates to modify protein charges.
  • Spectroscopic methods to measure binding affinity (K(a)) and electron transfer rate constants (k(et), k(2)).

Main Results:

  • Created a wide range of charge products (-q(Mb)q(b(5))) between ET partners.
  • Observed a 1000-fold increase in binding affinity with increasing -q(Mb)q(b(5)), showing exponential dependence.
  • Demonstrated a transition in electron transfer dynamics from fast to slow exchange with increasing charge interactions.
  • Validated the findings using data from the photosynthetic reaction center and cytochrome c(2) complex.

Conclusions:

  • Electrostatic interactions, particularly within a 'charged reactive patch,' dominate binding affinity and ET rates.
  • The engineered system provides a model for understanding electron transfer in protein complexes.
  • The observed trends are generalizable to other biologically relevant electron transfer systems.