Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB (Q27652023)

4

0 references

author name string

Goran Malojcić

1

0 references

Robin L Owen

2

0 references

John P A Grimshaw

Formation and transfer of disulphide bonds in living cells

3

0 references

language of work or name

English

0 references

publication date

15 October 2008

0 references

published in

FEBS Letters

0 references

volume

582

0 references

issue

23-24

0 references

page(s)

3301-7

0 references

cites work

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Recombinant protein folding and misfolding in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Identification of a protein required for disulfide bond formation in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Oxidative protein folding in bacteria

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Protein disulfide bond formation in prokaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Building bridges: disulphide bond formation in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

A pathway for disulfide bond formation in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Kinetic characterization of the disulfide bond-forming enzyme DsbB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Reaction mechanism for mammalian pyruvate dehydrogenase using natural lipoyl domain substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

X-ray study of baker's yeast lipoamide dehydrogenase at 4.5 A resolution by molecular replacement method

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Pathways for protein disulphide bond formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Protein disulfide isomerase: the structure of oxidative folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063

Enzymes catalyzing protein folding and their cellular functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.07.063