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

doi:10.1023/B:PRES.0000015407.61574.63

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	189-200
Number of pages	12
Journal	Photosynthesis Research
Volume	79
Issue number	2
DOIs	https://doi.org/10.1023/B:PRES.0000015407.61574.63
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

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10.1023/B:PRES.0000015407.61574.63

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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.",

keywords = "Alternate disulfide bonds, CN-induced cleavage, Fructose bisphosphatase, Light-activation, Mass mapping, Redox-regulation",

author = "Wei Wu and Watson, {J. Throck} and Stevens, {Fred J.} and Ryan Yousefzai and Anderson, {Louise E.}",

note = "Funding Information: We thank Renate Scheibe, Universit{\"a}t Osnabr{\"u}ck, Germany, for providing the recombinant spinach fructose bisphosphatase, Alex Dong Li for contributing the Molscript image of spinach fructose bisphos-phatase, and Lawrence Sykora and Jim Scios at the University of Illinois Chicago Greenhouse for cultivating the pea plants. This work was supported by a grant from the University of Illinois-Chicago Research Board (to L.E.A.) and by grant NIH R01GM60576 (to J.T.W.). Copyright: Copyright 2008 Elsevier B.V., All rights reserved.",

year = "2004",

doi = "10.1023/B:PRES.0000015407.61574.63",

language = "English (US)",

volume = "79",

pages = "189--200",

journal = "Photosynthesis Research",

issn = "0166-8595",

publisher = "Springer Netherlands",

number = "2",

}

TY - JOUR

T1 - Mass spectrometric evidence for an alternate disulfide bond in chloroplast fructose bisphosphatase

AU - Wu, Wei

AU - Watson, J. Throck

AU - Stevens, Fred J.

AU - Yousefzai, Ryan

AU - Anderson, Louise E.

N1 - Funding Information: We thank Renate Scheibe, Universität Osnabrück, Germany, for providing the recombinant spinach fructose bisphosphatase, Alex Dong Li for contributing the Molscript image of spinach fructose bisphos-phatase, and Lawrence Sykora and Jim Scios at the University of Illinois Chicago Greenhouse for cultivating the pea plants. This work was supported by a grant from the University of Illinois-Chicago Research Board (to L.E.A.) and by grant NIH R01GM60576 (to J.T.W.). Copyright: Copyright 2008 Elsevier B.V., All rights reserved.

PY - 2004

Y1 - 2004

N2 - 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.

AB - 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.

KW - Alternate disulfide bonds

KW - CN-induced cleavage

KW - Fructose bisphosphatase

KW - Light-activation

KW - Mass mapping

KW - Redox-regulation

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SN - 0166-8595

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EP - 200

JO - Photosynthesis Research

JF - Photosynthesis Research

IS - 2

ER -

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

Abstract

Keywords

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