Systematic re-evaluation of the bis(2-hydroxyethyl)disulfide (HEDS) assay reveals an alternative mechanism and activity of glutaredoxins-Reference-Cited by-同舟云学术

Systematic re-evaluation of the bis(2-hydroxyethyl)disulfide (HEDS) assay reveals an alternative mechanism and activity of glutaredoxins

Published:2015 Issue:7 Volume:6 Page:3788-3796
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Begas Patricia¹²³⁴,Staudacher Verena¹²³⁴,Deponte Marcel¹²³⁴

Affiliation:

1. Department of Parasitology

2. Ruprecht-Karls University

3. D-69120 Heidelberg

4. Germany

Abstract

The sequential kinetic patterns of mono- and dithiol glutaredoxins in the HEDS assay reflect an alternative enzymatic mechanism for the glutathione-dependent reduction of disulfide substrates.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/SC/C5SC01051A

Reference44 articles.

1. Thiotransferase in human red blood cells: kinetics and equilibrium

2. [29] Glutaredoxin

3. Two Novel Monothiol Glutaredoxins from Saccharomyces cerevisiae Provide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins

4. Glutaredoxins in Thiol/Disulfide Exchange

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