Identification of 2Fe-2S cysteine ligands in putidaredoxin

Nancy C. Gerber, Tadao Horiuchi, Hideo Koga, Stephen G. Sligar

Research output: Contribution to journalArticlepeer-review

Abstract

The iron-sulfur center of putidaredoxin is coordinated by four cysteine sulfhydrals. In order to determine which of the six cysteine residues in the protein coordinate the Fe-S center, we have individually mutated cysteine residues 73, 85 and 86 into serines. Of these mutant proteins, only C85S and C73S express holo-protein as evidenced by SDS-PAGE and EPR spectroscopy. This leads us to the conclusion that residues 39,45,48, and 86 are the cysteines that coordinate the iron-sulfur center in putidaredoxin.

Original languageEnglish (US)
Pages (from-to)1016-1020
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume169
Issue number3
DOIs
StatePublished - Jun 29 1990

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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