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K M Sendra1, A Barwinska-Sendra2, E S Mackenzie2

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Protein evolution shapes functional diversity, but natural metalloprotein studies are scarce. This research reveals how iron/manganese superoxide dismutases (SodFM) adapt metal preferences, showing evolutionary fine-tuning is key for enzyme activity.

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • Proteins are essential biological building blocks, with many enzymes requiring metal co-factors.
  • Metalloproteins often exhibit specific metal preferences, crucial for optimal function.
  • Environmental metal availability changes challenge metalloenzyme activity and drive evolution.

Purpose of the Study:

  • To investigate the evolution of metal preference in the iron/manganese superoxide dismutase (SodFM) family.
  • To identify key residues and evolutionary history influencing SodFM metal utilization.
  • To understand how SodFM enzymes adapt to varying metal bioavailability.

Main Methods:

  • Phylogenetic analysis of SodFM protein diversity.
  • Biochemical assays to determine metal preference and enzyme activity.
  • Structural biology to visualize metal-binding sites and evolutionary changes.

Main Results:

  • Identified conserved residues critical for determining SodFM metal preference.
  • Developed an improved predictive model for metal utilization based on evolutionary history.
  • Demonstrated that SodFM metal preference can be fine-tuned along a manganese-iron specificity scale.
  • Observed multiple independent modulations of SodFM metal preference throughout evolutionary history.

Conclusions:

  • SodFM metal preference is evolutionarily adaptable, allowing enzymes to maintain function under changing conditions.
  • Metal utilization in SodFM enzymes can shift over short evolutionary timescales.
  • Understanding these adaptations provides insights into protein evolution and metalloenzyme function.