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Article

An engineered pathway for the formation of protein disulfide bonds.

Science (New York, N.Y.) - 20 Feb 2004

Masip Lluis, Pan Jonathan L, Haldar Suranjana, Penner-Hahn James E, DeLisa Matthew P, Georgiou George, Bardwell James C A, Collet Jean-François

Abstract excerpt

We have engineered a pathway for the formation of disulfide bonds. By imposing evolutionary pressure, we isolated mutations that changed thioredoxin, which is a monomeric disulfide reductase, into a [2Fe-2S] bridged dimer capable of catalyzing O2-dependent sulfhydryl oxidation in vitro. Expression of the mutant protein in Escherichia coli with oxidizing cytoplasm and secretion via the Tat pathway restored...

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Identifiers

PMID: 14976313
DOI: 10.1126/science.1092612

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

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