Mass spectrometric evidence for an alternate disulfide bond in chloroplast fructose bisphosphatase

Wei Wu, J. Throck Watson, Fred J. Stevens, Ryan Yousefzai, Louise E. Anderson

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Mass mapping analysis based on cyanylation (CN) of the protein and CN-induced cleavage indicates that all three cysteine residues in the insertion into the light-activated pea leaf chloroplast fructose bisphosphatase (E.C. 3.1.3.11) are able to participate in disulfide bond formation. There is a major peak in the mass spectrum of the cleavage products indicating that Cys173 forms a disulfide bond with Cys153, consistent with the structure of the oxidized enzyme in PDB files 1d9q and 1dcu, and a minor peak indicating that Cys173 forms an alternate disulfide bond with Cys178. The Cys173-Cys178 disulfide bond was not apparent in the available crystal structures.

Original languageEnglish (US)
Pages (from-to)189-200
Number of pages12
JournalPhotosynthesis Research
Volume79
Issue number2
DOIs
StatePublished - 2004

Keywords

  • Alternate disulfide bonds
  • CN-induced cleavage
  • Fructose bisphosphatase
  • Light-activation
  • Mass mapping
  • Redox-regulation

ASJC Scopus subject areas

  • Biochemistry
  • Plant Science
  • Cell Biology

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