Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB. (Q34246180)

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15 January 2020

title

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

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15 January 2020

1

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15 January 2020

author name string

Yoh-hei Takahashi

series ordinal

2

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15 January 2020

Koreaki Ito

series ordinal

3

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15 January 2020

Shigehiko Hayashi

series ordinal

4

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15 January 2020

language of work or name

English

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publication date

29 December 2005

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15 January 2020

number of pages

6

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Proceedings of the National Academy of Sciences of the United States of America

inferred from page(s)

published in

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15 January 2020

volume

103

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15 January 2020

issue

2

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15 January 2020

page(s)

287-292

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The membrane-water interface region of membrane proteins: structural bias and the anti-snorkeling effect

15 January 2020

cites work

1 reference

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

6 July 2018

1 reference

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Mutational analysis of the disulfide catalysts DsbA and DsbB.

6 July 2018

1 reference

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Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria.

6 July 2018

1 reference

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Identification of a quinone-sensitive redox switch in the ArcB sensor kinase.

6 July 2018

1 reference

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

6 July 2018

1 reference

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

Mechanism of the electron transfer catalyst DsbB from Escherichia coli

6 July 2018

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The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase

6 July 2018

1 reference

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Protein disulfide bond formation in prokaryotes

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

Oxidative protein folding in bacteria

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

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

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase

6 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1323469

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

6 July 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

Reactivities of quinone-free DsbB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

DsbB catalyzes disulfide bond formation de novo

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

General atomic and molecular electronic structure system

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

Identification of a segment of DsbB essential for its respiration-coupled oxidation

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

Augmenter of liver regeneration: a flavin-dependent sulfhydryl oxidase with cytochrome c reductase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

Inter-Domain Redox Communication in Flavoenzymes of the Quiescin/Sulfhydryl Oxidase Family: Role of a Thioredoxin Domain in Disulfide Bond Formation,

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.0507570103

Disulfide bonds are generated by quinone reduction

21 January 2018

1 reference

12 December 2020

Lipoamide dehydrogenase from pig heart. Pyridine nucleotide induced changes in monoalkylated two-electron reduced enzyme

1 reference

12 December 2020

Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase

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12 December 2020

DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA

1 reference

12 December 2020

Oxidative protein folding is driven by the electron transport system

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12 December 2020

Identifiers

DOI

10.1073/PNAS.0507570103

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16384917%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

0 references

1 reference

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15 January 2020

PubMed publication ID

16384917

1 reference