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Article

Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways.

Proceedings of the National Academy of Sciences of the United States of America - 6 May 2008

Faulkner Melinda J, Veeravalli Karthik, Gon Stéphanie, Georgiou George, Beckwith Jon

Abstract excerpt

In Escherichia coli, the glutathione/glutaredoxin and thioredoxin pathways are essential for the reduction of cytoplasmic protein disulfide bonds, including those formed in the essential enzyme ribonucleotide reductase during its action on substrates. Double mutants lacking thioredoxin reductase (trxB) and glutathione reductase (gor) or glutathione biosynthesis (gshA) cannot grow. Growth of Deltagor DeltatrxB...

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Identifiers

PMID: 18456836
DOI: 10.1073/pnas.0801986105
PMCID: PMC2373332

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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