title: Mass Spectrometric Evidence for an Alternate Disulfide Bond in Chloroplast Fructose Bisphosphatase.
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.
authors.affiliation: Department of Chemistry, Michigan State University, East Lansing, MI, 48824, USA.
authors.forename: Wei
authors.initials: W
authors.lastname: Wu
authors.affiliation: Department of Chemistry, Michigan State University, East Lansing, MI, 48824, USA.
authors.forename: J Throck
authors.initials: JT
authors.lastname: Watson
authors.affiliation: Biosciences Division, Argonne National Laboratory, Argonne, IL, 60439, USA.
authors.forename: Fred J
authors.initials: FJ
authors.lastname: Stevens
authors.affiliation: Department of Biological Sciences, University of Illinois-Chicago, 845 West Taylor, Chicago, IL, 60680, USA.|Department of Chemistry, University of Illinois-Chicago, 845 West Taylor, Chicago, IL, 60680, USA.
authors.forename: Ryan
authors.initials: R
authors.lastname: Yousefzai
authors.affiliation: Department of Biological Sciences, University of Illinois-Chicago, 845 West Taylor, Chicago, IL, 60680, USA.|Department of Chemistry, University of Illinois-Chicago, 845 West Taylor, Chicago, IL, 60680, USA.
authors.forename: Louise E
authors.initials: LE
authors.lastname: Anderson