Characterization of purified c-type heme-containing peptides and identification of c-type heme-attachment sites in Shewanella oneidenis cytochromes using mass spectrometry

J Proteome Res. 2005 May-Jun;4(3):846-54. doi: 10.1021/pr0497475.

Abstract

We describe methods for mass spectrometric identification of heme-containing peptides from c-type cytochromes that contain the CXXCH (X=any amino acid) sequence motif. The heme fragment ion yielded the most abundant MS/MS peak for standard heme-containing peptides with one amino acid difference for both 2+ and 3+ peptide charge states; both sequence and charge affect the extent of heme loss. Application to Shewanella oneidenis demonstrated the utility of this approach for identifying c-type heme-containing peptides from complex proteome samples.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacterial Proteins / analysis*
  • Binding Sites
  • Cytochrome c Group / analysis*
  • Heme
  • Mass Spectrometry
  • Peptide Fragments / isolation & purification
  • Shewanella / chemistry*

Substances

  • Bacterial Proteins
  • Cytochrome c Group
  • Peptide Fragments
  • Heme