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Related Experiment Videos

Redox-dependent conformational selection in a Cys4Fe2S2 ferredoxin.

T C Pochapsky1, M Kostic, N Jain

  • 1Departments of Chemistry and Biochemistry, Brandeis University, Waltham, Massachusetts 02254-9110.

Biochemistry
|May 9, 2001
PubMed
Summary

Putidaredoxin

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Area of Science:

  • Biochemistry
  • Protein Dynamics
  • Redox Biology

Background:

  • Putidaredoxin (Pdx) is a ferredoxin involved in electron transfer.
  • Pdx exhibits redox-dependent binding to cytochrome P450(cam) (CYP101).
  • The reduced form of Pdx (Pdx(r)) binds more strongly to CYP101 than the oxidized form (Pdx(o)).

Purpose of the Study:

  • To investigate the mechanism of redox-dependent conformational selection in Pdx.
  • To elucidate the role of the metal cluster binding loop in Pdx dynamics.
  • To provide direct evidence for redox-dependent conformational ensembles.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy (15N and 13C resonances).
  • Paramagnetic relaxation effects.
  • Site-directed mutagenesis (G40N mutation in Pdx).

Main Results:

  • The metal cluster binding loop is the primary determinant of redox-dependent conformational changes in Pdx.
  • Upon reduction, the metal cluster binding loop contracts, reducing Pdx dynamics.
  • A G40N mutation allows direct observation of slow conformational exchange in Pdx(o).
  • Pdx(r) populates fewer conformational substates than Pdx(o), confirming conformational selection.

Conclusions:

  • Conformational selection within the Fe2S2 cluster binding loop drives redox-dependent protein dynamics in Pdx.
  • These findings offer a mechanism for coupling Pdx oxidation state to CYP101 binding affinity.
  • This study provides the first direct observation of slow-exchange, redox-dependent conformational ensembles.

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