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

Theoretical Chemistry

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

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.

PY - 2008

Y1 - 2008

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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

U2 - 10.1021/jp7104665

DO - 10.1021/jp7104665

M3 - Article

SN - 1520-6106

VL - 112

SP - 2511

EP - 2523

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 8

ER -

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

Abstract

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