A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity. (Q46061616)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19345687%20AND%20SRC:MED&resulttype=core&format=json

25 January 2020

title

A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity (English)

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25 January 2020

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25 January 2020

Juan Manuel Perez Ruiz

series ordinal

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25 January 2020

author name string

Juan Manuel Pérez-Ruiz

series ordinal

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19 December 2017

http://europepmc.org/abstract/MED/19345687

language of work or name

English

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publication date

5 April 2009

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25 January 2020

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25 January 2020

volume

583

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issue

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page(s)

1399-1402

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Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals?

25 January 2020

cites work

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Unique properties of NADP-thioredoxin reductase C in legumes.

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NADPH Thioredoxin reductase C controls the redox status of chloroplast 2-Cys peroxiredoxins in Arabidopsis thaliana

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NONPHOTOSYNTHETIC METABOLISM IN PLASTIDS.

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NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mg-protoporphyrin monomethyl ester cyclase

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

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The quaternary structure of NADPH thioredoxin reductase C is redox-sensitive

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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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