The role of Arginine 38 in horseradish peroxidase enzyme revisited: A computational investigation

2009 ◽  
Vol 141 (1) ◽  
pp. 87-93 ◽  
Author(s):  
Simone Tatoli ◽  
Costantino Zazza ◽  
Nico Sanna ◽  
Amedeo Palma ◽  
Massimiliano Aschi
2013 ◽  
Vol 67 (3) ◽  
pp. 419-426
Author(s):  
Vladan Djuric ◽  
Nebojsa Deletic ◽  
Vesna Stankov-Jovanovic ◽  
Ranko Simonovic

Primary role of peroxidase enzyme is to decompose endogenous hydrogen peroxide, when oxygen radical is being replaced by a less potent radical, which is its cosubstrates oxidized form. During this study, catalytic activity of horseradish peroxidase has been observed in the presence of antioxidants from vitamin group, such as C, E and A, i.e. their water-soluble forms. It was found that vitamin E showed no effect on the enzyme activity and fate of cosubstrate radicals from the group of benzidine derivatives. Vitamin C proceeds enzymatic reaction showing its antioxidative character, and absorbs electrons from radicals, bringing cosubstrate back to its relaxed state. On the other hand, vitamin A plays a role of uncompetitive peroxidase inhibitor, which is visible through decreasing initial rate of catalytic reaction, and is reflected as virtual decrease of enzyme concentration. Furthermore, it prolongs life of endogenous hydrogen peroxide, which could potentially lead to oxidative stress of cells. This inhibitory effect can be used in analytical purpose, for determination of retinol acetate content in a sample.


ChemPhysChem ◽  
2016 ◽  
Vol 17 (23) ◽  
pp. 3948-3953 ◽  
Author(s):  
Tainah Dorina Marforio ◽  
Andrea Bottoni ◽  
Matteo Calvaresi ◽  
Daniele Fabbri ◽  
Pietro Giacinto ◽  
...  

2018 ◽  
Vol 10 (23) ◽  
pp. 2731-2739 ◽  
Author(s):  
Amir Kaffash ◽  
Hamid R. Zare ◽  
Khosrow Rostami

An electrochemically reduced graphene oxide and horseradish peroxidase enzyme modified electrode has been used for phenol determination.


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