(Q27652023)

4

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author name string

Goran Malojcić

1

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Robin L Owen

2

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John P A Grimshaw

Formation and transfer of disulphide bonds in living cells

3

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language of work or name

English

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publication date

15 October 2008

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published in

FEBS Letters

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volume

582

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issue

23-24

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page(s)

3301-7

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cites work

1 reference

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The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis.

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Identification of a protein required for disulfide bond formation in vivo

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Oxidative protein folding in bacteria

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Protein disulfide bond formation in prokaryotes

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The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

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Building bridges: disulphide bond formation in the cell

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A pathway for disulfide bond formation in vivo

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Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway

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Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells

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Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo

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Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA

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Kinetic characterization of the disulfide bond-forming enzyme DsbB.

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Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.

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Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.

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Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli

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Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.

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DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.

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Disulfide bond formation involves a quinhydrone-type charge–transfer complex

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Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell

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A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p

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The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases

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