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Veronica Tamu Dufe on Muck Rack

Veronica Tamu Dufe

As seen in: The Journal of Biological Chemistry
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Articles

Sulfur denitrosylation by an engineered Trx-like DsbG enzyme identifies nucleophilic cysteine hydrogen bonds as key functional determinant.

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By Celine Lafaye, Veronica Tamu Dufe, Khadija Wahni, Ariane Boudier
| The Journal of Biological Chemistry Verified
Sulfur denitrosylation by an engineered Trx-like DsbG enzyme identifies nucleophilic cysteine hydrogen bonds as key functional determinant. VOLUME 291 (2016) PAGES 15020–15028 Table 2 was inadvertently omitted in the version of this article that was published on July 15, 2016. This error has now been corrected. Table 2 X-ray data collection, processing, and refinement statistics © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.
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Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant

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By Celine Lafaye, Vrije Universiteit Brussel, Veronica Tamu Dufe, Khadija Wahni
| The Journal of Biological Chemistry Verified
Exposure of bacteria to NO results in the nitrosylation of cysteine thiols in proteins and low molecular weight thiols such as GSH. The cells possess enzymatic systems that catalyze the denitrosylation of these modified sulfurs. An important player in these systems is thioredoxin (Trx), a ubiquitous, cytoplasmic oxidoreductase that can denitrosylate proteins in vivo and S-nitrosoglutathione (GSNO) in vitro.
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Sulfur denitrosylation by an engineered Trx-like DsbG enzyme identifies nucleophilic cysteine hydrogen bonds as key functional determinant

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By Celine Lafaye, Veronica Tamu Dufe, Khadija Wahni, Ariane Boudier, Pierre Leroy
| The Journal of Biological Chemistry Verified
Exposure of bacteria to nitric oxide (NO) results in the nitrosylation of cysteine thiols in proteins and low molecular weight thiols such as glutathione (GSH). Cells possess enzymatic systems that catalyze the denitrosylation of these modified sulfurs. An important player in these systems is thioredoxin (Trx), a ubiquitous, cytoplasmic oxidoreductase that can denitrosylate proteins in vivo and S-nitrosoglutathione (GSNO) in vitro.
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