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Multimodal Response to Copper Binding in Superoxide Dismutase Dynamics.

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Copper/zinc superoxide dismutase (SOD) dynamics were studied in two metalated forms. Metal ion uptake modulates protein flexibility, influencing motion across various timescales.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Structural Biology

Background:

  • Copper/zinc superoxide dismutase (SOD) is a crucial metalloenzyme implicated in amyotrophic lateral sclerosis.
  • Understanding SOD's structure-function relationship is vital for neurodegenerative disease research.

Purpose of the Study:

  • To investigate the impact of metalation on SOD dynamics.
  • To quantify protein motions in different metalated states of SOD.

Main Methods:

  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Fast magic-angle spinning (MAS) at high magnetic fields (800-1000 MHz).
  • Analysis of microcrystalline preparations of Cu,Zn-SOD and E,Zn-SOD.

Main Results:

  • Metal ion uptake does not rigidify SOD but redistributes motional processes.
  • Motions were quantified across a dynamic range from nanoseconds to milliseconds.
  • Coupling between histidine side chain dynamics and remote backbone elements was observed.

Conclusions:

  • Metalation state significantly influences the dynamic landscape of SOD.
  • SOD's flexibility is finely tuned by metal ion incorporation, affecting protein function.
  • These findings offer insights into SOD's role in disease mechanisms.