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 language | English (US) |
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Pages (from-to) | 189-200 |
Number of pages | 12 |
Journal | Photosynthesis Research |
Volume | 79 |
Issue number | 2 |
DOIs | |
State | Published - 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