Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin (Q24598311)

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English	Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin	scientific article

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Europe PubMed Central

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3832347

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4 January 2020

title

Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin (English)

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Europe PubMed Central

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3832347

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4 January 2020

author

Paul Karplus

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5

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3832347

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4 January 2020

Leslie B Poole

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6

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3832347

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4 January 2020

author name string

Derek Parsonage

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1

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3832347

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4 January 2020

Derek S Youngblood

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2

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3832347

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4 January 2020

Ganapathy N Sarma

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3

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3832347

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4 January 2020

Zachary A Wood

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4

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3832347

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language of work or name

English

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publication date

1 August 2005

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3832347

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4 January 2020

published in

Biochemistry

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3832347

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4 January 2020

volume

44

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3832347

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4 January 2020

issue

31

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3832347

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4 January 2020

page(s)

10583-10592

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3832347

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4 January 2020

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Structure, mechanism and regulation of peroxiredoxins

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Peroxiredoxins

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PubMed Central

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27 September 2017

Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization

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AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase

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27 September 2017

Divergence of function in the thioredoxin fold suprafamily: evidence for evolution of peroxiredoxins from a thioredoxin-like ancestor

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AhpF can be dissected into two functional units: tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC.

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Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein

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Crystal structure of a novel Plasmodium falciparum 1-Cys peroxiredoxin

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Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity.

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Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase

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Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins

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Tryptophan fluorescence study of conformational transitions of the oxidized and reduced form of thioredoxin

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Identifiers

DOI

10.1021/BI050448I

2 references

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4418664

stated in

Europe PubMed Central

PMC publication ID

3832347

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16060667%20AND%20SRC:MED&resulttype=core&format=json

retrieved

4 January 2020

OpenCitations bibliographic resource ID

4418664

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4418664

PMC publication ID

3832347

2 references

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4418664

stated in

Europe PubMed Central

PMC publication ID

3832347

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16060667%20AND%20SRC:MED&resulttype=core&format=json

retrieved

4 January 2020

PubMed publication ID

16060667

2 references

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4418664

stated in

Europe PubMed Central

PMC publication ID

3832347

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16060667%20AND%20SRC:MED&resulttype=core&format=json

retrieved

4 January 2020

ResearchGate publication ID

7686240

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