Calculation of Cys 30 δpKa's and oxidising power for DsbA mutants

J. Warwicker; P. J. Gane

doi:10.1016/0014-5793(96)00358-4

Calculation of Cys 30 δpKa's and oxidising power for DsbA mutants

Research output: Contribution to journal › Article › peer-review

Abstract

DsbA possesses a redox active disulphide, with the equilibrium strongly shifted towards the reduced form as compared to its structural homologue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power within the thioredoxin family. Data concerning redox and pKa properties for DsbA mutants in this region are available. Electrostatics calculations show reasonable agreement with the experimental data, and support the suggestion that amino acids outside of the CXXC active site sequence are as important in determining oxidising power within the thioredoxin family as are those within it.

Original language	English
Pages (from-to)	105-108
Number of pages	3
Journal	FEBS Letters
Volume	385
Issue number	1-2
DOIs	https://doi.org/10.1016/0014-5793(96)00358-4
Publication status	Published - 29 Apr 1996

Keywords

Disulphide bridge
Electrostatic interaction
Molecular modelling
Redox potential
Thioredoxin

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10.1016/0014-5793(96)00358-4

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title = "Calculation of Cys 30 δpKa's and oxidising power for DsbA mutants",

abstract = "DsbA possesses a redox active disulphide, with the equilibrium strongly shifted towards the reduced form as compared to its structural homologue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power within the thioredoxin family. Data concerning redox and pKa properties for DsbA mutants in this region are available. Electrostatics calculations show reasonable agreement with the experimental data, and support the suggestion that amino acids outside of the CXXC active site sequence are as important in determining oxidising power within the thioredoxin family as are those within it.",

keywords = "Disulphide bridge, Electrostatic interaction, Molecular modelling, Redox potential, Thioredoxin",

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T1 - Calculation of Cys 30 δpKa's and oxidising power for DsbA mutants

AU - Warwicker, J.

AU - Gane, P. J.

PY - 1996/4/29

Y1 - 1996/4/29

N2 - DsbA possesses a redox active disulphide, with the equilibrium strongly shifted towards the reduced form as compared to its structural homologue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power within the thioredoxin family. Data concerning redox and pKa properties for DsbA mutants in this region are available. Electrostatics calculations show reasonable agreement with the experimental data, and support the suggestion that amino acids outside of the CXXC active site sequence are as important in determining oxidising power within the thioredoxin family as are those within it.

AB - DsbA possesses a redox active disulphide, with the equilibrium strongly shifted towards the reduced form as compared to its structural homologue, thioredoxin. It is widely believed that the two amino acids that separate the active site cysteines play a crucial role in determining oxidising power within the thioredoxin family. Data concerning redox and pKa properties for DsbA mutants in this region are available. Electrostatics calculations show reasonable agreement with the experimental data, and support the suggestion that amino acids outside of the CXXC active site sequence are as important in determining oxidising power within the thioredoxin family as are those within it.

KW - Disulphide bridge

KW - Electrostatic interaction

KW - Molecular modelling

KW - Redox potential

KW - Thioredoxin

U2 - 10.1016/0014-5793(96)00358-4

DO - 10.1016/0014-5793(96)00358-4

M3 - Article

C2 - 8641451

VL - 385

SP - 105

EP - 108

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

Calculation of Cys 30 δpKa's and oxidising power for DsbA mutants

Abstract

Keywords

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