Glutaredoxins in Thiol/Disulfide Exchange

2013 ◽  
Vol 18 (13) ◽  
pp. 1654-1665 ◽  
Author(s):  
Christopher Horst Lillig ◽  
Carsten Berndt
Keyword(s):  
Disulfide Exchange

Pyridyl disulfide-based thiol–disulfide exchange reaction: shaping the design of redox-responsive polymeric materials

2020 ◽  
Vol 11 (48) ◽  
pp. 7603-7624
Author(s):  
Ismail Altinbasak ◽  
Mehmet Arslan ◽  
Rana Sanyal ◽  
Amitav Sanyal
Keyword(s):  
Exchange Reaction ◽  
Functional Materials ◽  
Polymeric Materials ◽  
Disulfide Exchange ◽  
Redox Responsive ◽  
Synthetic Approaches

This review provides an overview of synthetic approaches utilized to incorporate the thiol-reactive pyridyl-disulfide motif into various polymeric materials, and briefly highlights its utilization to obtain functional materials.

scholarly journals Adventures in molecular recognition. The ins and outs of templating

2000 ◽  
Vol 72 (12) ◽  
pp. 2265-2274 ◽  
Author(s):  
Jeremy K. M. Sanders
Keyword(s):  
Molecular Recognition ◽  
Combinatorial Chemistry ◽  
Biological Systems ◽  
Design Approach ◽  
Supramolecular Systems ◽  
Disulfide Exchange ◽  
Dynamic Combinatorial Chemistry ◽  
Evolutionary Features ◽  
Selection Approach ◽  
Porphyrin Dimers

Two different approaches are described for the creation of supramolecular systems potentially capable of recognition and catalysis. Using the design approach, we have been able to accelerate and influence two different Diels­Alder reactions within the cavities of porphyrin dimers and trimers; this is templating from the outside inwards. The selection approach is a synthetic chemical attempt to capture some of the key evolutionary features of biological systems: dynamic combinatorial chemistry is used to create equilibrating mixtures of potential receptors, and then a template is used to select and amplify the desired system. Five potential reactions for such dynamic chemistry are discussed: base-catalyzed transesterification, hydrazone exchange, disulfide exchange, alkene metathesis, and Pd-catalyzed allyl exchange, and preliminary templating results (inside outwards) are presented.

Large-Scale Capture of Peptides Containing Reversibly Oxidized Cysteines by Thiol-Disulfide Exchange Applied to the Myocardial Redox Proteome

2013 ◽  
Vol 85 (7) ◽  
pp. 3774-3780 ◽  
Author(s):  
Jana Paulech ◽  
Nestor Solis ◽  
Alistair V.G. Edwards ◽  
Max Puckeridge ◽  
Melanie Y. White ◽  
...  
Keyword(s):  
Large Scale ◽  
Disulfide Exchange

scholarly journals A “molten globule” of Torpedo acetylcholinesterase undergoes thiol-disulfide exchange.

1994 ◽  
Vol 269 (48) ◽  
pp. 30093-30096
Author(s):  
J Eichler ◽  
D.I. Kreimer ◽  
L Varon ◽  
I Silman ◽  
L Weiner
Keyword(s):  
Molten Globule ◽  
Disulfide Exchange

scholarly journals Glutaredoxins employ parallel monothiol–dithiol mechanisms to catalyze thiol–disulfide exchanges with protein disulfides

2018 ◽  
Vol 9 (5) ◽  
pp. 1173-1183 ◽  
Author(s):  
Ashwinie A. Ukuwela ◽  
Ashley I. Bush ◽  
Anthony G. Wedd ◽  
Zhiguang Xiao
Keyword(s):  
Disulfide Exchange ◽  
Protein Disulfides

Glutaredoxins were demonstrated to be a family of versatile enzymes capable of catalyzing thiol–disulfide exchange involving GSSG/GSH via different catalytic routes either alone or in parallel.

Enrichment of O-GlcNAc-modified peptides using novel thiol-alkyne and thiol-disulfide exchange

2015 ◽  
Vol 25 (13) ◽  
pp. 2645-2649 ◽  
Author(s):  
Hiroki Tsumoto ◽  
Daisuke Ogasawara ◽  
Noritaka Hashii ◽  
Takayoshi Suzuki ◽  
Yoshihiro Akimoto ◽  
...  
Keyword(s):  
Disulfide Exchange ◽  
Modified Peptides

scholarly journals Mitochondrial Thioredoxin-Glutathione Reductase from LarvalTaenia crassiceps(Cysticerci)

2010 ◽  
Vol 2010 ◽  
pp. 1-11 ◽  
Author(s):  
Alberto Guevara-Flores ◽  
Irene P. del Arenal ◽  
Guillermo Mendoza-Hernández ◽  
Juan Pablo Pardo ◽  
Oscar Flores-Herrera ◽  
...  
Keyword(s):  
Glutathione Reductase ◽  
Reductase Activity ◽  
Catalytic Efficiency ◽  
Dependent Manner ◽  
Exchange Reactions ◽  
Disulfide Exchange ◽  
Oxidative Inactivation ◽  
Disulfide Reductase ◽  
Thioredoxin Peroxidase ◽  
Thioredoxin Glutathione Reductase

Mitochondrial thioredoxin-glutathione reductase was purified from larvalTaenia crassiceps(cysticerci). The preparation showed NADPH-dependent reductase activity with either thioredoxin or GSSG, and was able to perform thiol/disulfide exchange reactions. At25∘Cspecific activities were437  ±  27mU mg-1and840  ±  49mU mg-1with thioredoxin and GSSG, respectively. ApparentKmvalues were0.87  ±  0.04 μM,41  ±  6 μM and19  ±  10 μM for thioredoxin, GSSG and NADPH, respectively. Thioredoxin from eukaryotic sources was accepted as substrate. The enzyme reduced H2O2in a NADPH-dependent manner, although with low catalytic efficiency. In the presence of thioredoxin, mitochondrial TGR showed a thioredoxin peroxidase-like activity. All disulfide reductase activities were inhibited by auranofin, suggesting mTGR is dependent on selenocysteine. The reductase activity with GSSG showed a higher dependence on temperature as compared with the DTNB reductase activity. The variation of the GSSG- and DTNB reductase activities on pH was dependent on the disulfide substrate. Like the cytosolic isoform, mTGR showed a hysteretic kinetic behavior at moderate or high GSSG concentrations, but it was less sensitive to calcium. The enzyme was able to protect glutamine synthetase from oxidative inactivation, suggesting that mTGR is competent to contend with oxidative stress.

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