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Issue 12, 2015
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The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity

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Abstract

Thiol–disulfide oxidoreductases from the thioredoxin (Trx) family of proteins have a broad range of well documented functions and possess distinct substrate specificities. The mechanisms and characteristics that control these specificities are key to the understanding of both the reduction of catalytic disulfides as well as allosteric disulfides (thiol switches). Here, we have used the catalytic disulfide of E. coli 3′-phosphoadenosine 5′-phosphosulfate (PAPS) reductase (PR) that forms between the single active site thiols of two monomers during the reaction cycle as a model system to investigate the mechanisms of Trx and Grx protein specificity. Enzyme kinetics, ΔE0 determination, and structural analysis of various Trx and Grx family members suggested that the redox potential does not determine specificity nor efficiency of the redoxins as reductant for PR. Instead, the efficiency of PR with various redoxins correlated strongly to the extent of a negative electric field of the redoxins reaching into the solvent outside the active site, and electrostatic and geometric complementary contact surfaces. These data suggest that, in contrast to common assumption, the composition of the active site motif is less important for substrate specificity than other amino acids in or even outside the immediate contact area.

Graphical abstract: The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity

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Article information


Submitted
24 Apr 2015
Accepted
08 Sep 2015
First published
09 Sep 2015

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2015,6, 7049-7058
Article type
Edge Article
Author version available

The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity

C. Berndt, J. Schwenn and C. H. Lillig, Chem. Sci., 2015, 6, 7049
DOI: 10.1039/C5SC01501D

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

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    [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
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    [Original citation] - Published by The Royal Society of Chemistry.

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