Redox-dependent conformational selection in a Cys4Fe2S2 ferredoxin.

  title={Redox-dependent conformational selection in a Cys4Fe2S2 ferredoxin.},
  author={T. Pochapsky and M. Kostic and N. Jain and R. Pejchal},
  volume={40 19},
  • T. Pochapsky, M. Kostic, +1 author R. Pejchal
  • Published 2001
  • Chemistry, Medicine
  • Biochemistry
  • Putidaredoxin (Pdx), a Cys4Fe2S2 ferredoxin from Pseudomonas putida, exhibits redox-dependent binding to its physiological redox partner, cytochrome P450(cam) (CYP101), with the reduced form of Pdx (Pdx(r)) binding with greater affinity to oxidized camphor-bound CYP101 than the oxidized form, Pdx(o). It has been previously shown that Pdx(o) is more dynamic than Pdx(r) on all accessible time scales, and it has been proposed that Pdx(r) samples only a fraction of the conformational substates… CONTINUE READING
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