Mass Spectrometric Evidence for an Alternate Disulfide Bond in Chloroplast Fructose Bisphosphatase |
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Authors: | Wei Wu J Throck Watson Fred J Stevens Ryan Yousefzai Louise E Anderson |
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Institution: | Department of Chemistry, Michigan State University, East Lansing, MI, 48824, USA. |
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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. |
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Keywords: | alternate disulfide bonds CN-induced cleavage fructose bisphosphatase light-activation mass mapping redox-regulation |
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