scholarly journals Enzymatic Antioxidant Signatures in Hyperthermophilic Archaea

Antioxidants ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 703 ◽  
Author(s):  
Emilia Pedone ◽  
Gabriella Fiorentino ◽  
Simonetta Bartolucci ◽  
Danila Limauro

To fight reactive oxygen species (ROS) produced by both the metabolism and strongly oxidative habitats, hyperthermophilic archaea are equipped with an array of antioxidant enzymes whose role is to protect the biological macromolecules from oxidative damage. The most common ROS, such as superoxide radical (O2•−) and hydrogen peroxide (H2O2), are scavenged by superoxide dismutase, peroxiredoxins, and catalase. These enzymes, together with thioredoxin, protein disulfide oxidoreductase, and thioredoxin reductase, which are involved in redox homeostasis, represent the core of the antioxidant system. In this review, we offer a panorama of progression of knowledge on the antioxidative system in aerobic or microaerobic (hyper)thermophilic archaea and possible industrial applications of these enzymes.

1980 ◽  
Vol 255 (23) ◽  
pp. 11085-11087
Author(s):  
J. Moss ◽  
S.J. Stanley ◽  
J.E. Morin ◽  
J.E. Dixon

2006 ◽  
Vol 356 (1) ◽  
pp. 155-164 ◽  
Author(s):  
Emilia Pedone ◽  
Katia D'Ambrosio ◽  
Giuseppina De Simone ◽  
Mosè Rossi ◽  
Carlo Pedone ◽  
...  

1972 ◽  
Vol 50 (5) ◽  
pp. 507-509 ◽  
Author(s):  
Luis A. Branda ◽  
Barbara M. Ferrier ◽  
Lynne Celhoffer

Thiol–protein disulfide oxidoreductase activity was detected in the soluble cell fraction of human placental tissue homogenized in sucrose. This activity was demonstrated in the rapid reduction of oxytocin and the somewhat less rapid reduction of insulin by reduced glutathione. The apparent pH optimum of the enzymic activity for the reduction of oxytocin and insulin was found to be near pH 8.


2005 ◽  
Vol 61 (a1) ◽  
pp. c206-c206
Author(s):  
K. D'Ambrosia ◽  
G. De Simone ◽  
E. Pedone ◽  
M. Rossi ◽  
S. Bartolucci ◽  
...  

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