(Q33712972)

28 July 2017

title

Disulfide bond formation involves a quinhydrone-type charge-transfer complex (English)

1 reference

28 July 2017

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

1 reference

DOI

10.1073/PNAS.1935988100

https://api.crossref.org/works/10.1073/PNAS.1935988100

31 March 2024

3

Bernard L Trumpower

1 reference

28 July 2017

James Regeimbal

1

1 reference

28 July 2017

Stefan Gleiter

2

1 reference

28 July 2017

Chang-An Yu

4

1 reference

28 July 2017

Mithun Diwakar

5

1 reference

28 July 2017

David P. Ballou

6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14612576

31 March 2024

James C. A. Bardwell

7

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14612576

31 March 2024

language of work or name

English

0 references

publication date

11 November 2003

1 reference

full work available at URL

28 July 2017

https://europepmc.org/articles/pmc283498?pdf=render

file format

Portable Document Format

online access status

open access

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14612576

https://europepmc.org/articles/PMC283498

31 March 2024

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14612576

https://europepmc.org/articles/PMC283498?pdf=render

31 March 2024

file format

Portable Document Format

online access status

open access

content deliverer

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14612576

https://doi.org/10.1073/pnas.1935988100

31 March 2024

online access status

open access

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14612576

https://pnas.org/doi/pdf/10.1073/pnas.1935988100

31 March 2024

1 reference

DOI

10.1073/PNAS.1935988100

https://api.crossref.org/works/10.1073/PNAS.1935988100

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

31 March 2024

published in

1 reference

28 July 2017

volume

100

1 reference

28 July 2017

issue

24

1 reference

28 July 2017

page(s)

13779-13784

1 reference

Mechanism of the electron transfer catalyst DsbB from Escherichia coli

28 July 2017

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

Protein disulfide bond formation in prokaryotes

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

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

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

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

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

Oxidative protein folding in bacteria

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

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

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

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

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

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

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

Bifurcated ubihydroquinone oxidation in the cytochrome bc1 complex by proton-gated charge transfer.

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

A pathway for disulfide bond formation in vivo

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

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

21 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=283498

DsbB catalyzes disulfide bond formation de novo

21 June 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

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.1935988100

Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Complex II from phototrophic purple bacterium Rhodoferax fermentans displays rhodoquinol-fumarate reductase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Ubiquinone pair in the Qo site central to the primary energy conversion reactions of cytochrome bc1 complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Three molecules of ubiquinone bind specifically to mitochondrial cytochrome bc1 complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Oxidative protein folding is driven by the electron transport system

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Disulfide bonds are generated by quinone reduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

A hydroxyquinone with amine oxidase activity: preparation and properties

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Free-living nematodes Caenorhabditis elegans possess in their mitochondria an additional rhodoquinone, an essential component of the eukaryotic fumarate reductase system

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Proton-coupled electron transfer at the Q(o) site: what type of mechanism can account for the high activation barrier?

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

Reconstitution of a protein disulfide catalytic system

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1935988100

21 January 2018

Identifiers

DOI

10.1073/PNAS.1935988100

1 reference

28 July 2017

0 references

1 reference

28 July 2017

1 reference