Mechanism of thioredoxin-catalyzed disulfide reduction. Activation of the buried thiol and role of the variable active-site residues

A.P. Carvalho; M. Swart; J.N.P. van Stralen; P.A. Fernandes; M.E. Ramos; F.M. Bickelhaupt

doi:10.1021/jp7104665

Mechanism of thioredoxin-catalyzed disulfide reduction. Activation of the buried thiol and role of the variable active-site residues

A.P. Carvalho, M. Swart, J.N.P. van Stralen, P.A. Fernandes, M.E. Ramos, F.M. Bickelhaupt

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Thioredoxins (Trx) are enzymes with a characteristic CXYC active-site motif that catalyze the reduction of disulfide bonds in other proteins. We have theoretically explored this reaction mechanism, both in the gas phase and in water, using density functional theory. The mechanism of disulfide reduction involves two consecutive thiol-disulfide exchange reactions, that is, nucleophilic substitutions at sulfur (S

Original language	English
Pages (from-to)	2511-23
Journal	Journal of Physical Chemistry B
Volume	112
Issue number	8
DOIs	https://doi.org/10.1021/jp7104665
Publication status	Published - 2008

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abstract = "Thioredoxins (Trx) are enzymes with a characteristic CXYC active-site motif that catalyze the reduction of disulfide bonds in other proteins. We have theoretically explored this reaction mechanism, both in the gas phase and in water, using density functional theory. The mechanism of disulfide reduction involves two consecutive thiol-disulfide exchange reactions, that is, nucleophilic substitutions at sulfur (S",

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AU - Carvalho, A.P.

AU - Swart, M.

AU - van Stralen, J.N.P.

AU - Fernandes, P.A.

AU - Ramos, M.E.

AU - Bickelhaupt, F.M.

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AB - Thioredoxins (Trx) are enzymes with a characteristic CXYC active-site motif that catalyze the reduction of disulfide bonds in other proteins. We have theoretically explored this reaction mechanism, both in the gas phase and in water, using density functional theory. The mechanism of disulfide reduction involves two consecutive thiol-disulfide exchange reactions, that is, nucleophilic substitutions at sulfur (S

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Mechanism of thioredoxin-catalyzed disulfide reduction. Activation of the buried thiol and role of the variable active-site residues

Abstract

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