Chapter title |
Carbonate Anion Radical Generated by the Peroxidase Activity of Copper-Zinc Superoxide Dismutase: Scavenging of Radical and Protection of Enzyme by Hypotaurine and Cysteine Sulfinic Acid
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Chapter number | 43 |
Book title |
Taurine 10
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Published in |
Advances in experimental medicine and biology, January 2017
|
DOI | 10.1007/978-94-024-1079-2_43 |
Pubmed ID | |
Book ISBNs |
978-9-40-241077-8, 978-9-40-241079-2
|
Authors |
Alessia Baseggio Conrado, Simonetta Maina, Harry Moseley, Antonio Francioso, Luciana Mosca, Elisabetta Capuozzo, Mario Fontana |
Abstract |
Copper-zinc superoxide dismutase (SOD) is considered one of the most important mammalian antioxidant defenses and plays a relevant role due to its main function in catalyzing the dismutation of superoxide anion to oxygen and hydrogen peroxide. However, interaction between SOD and H2O2 produced a strong copper-bound oxidant (Cu(II)(•)OH) that seems able to contrast the self-inactivation of the enzyme or oxidize other molecules through its peroxidase activity. The bicarbonate presence enhances the peroxidase activity and produces the carbonate anion radical (CO3(•-)). CO3(•-) is a freely diffusible reactive species capable of oxidizing several molecules that are unwieldy to access into the reactive site of the enzyme. Cu(II)(•)OH oxidizes bicarbonate to the CO3(•-), which spreads out of the binding site and oxidizes hypotaurine and cysteine sulfinic acid to the respective sulfonates through an efficient reaction. These findings suggest a defense role for sulfinates against the damage caused by CO3(•-) . The effect of hypotaurine and cysteine sulfinic acid on the CO3(•-)-mediated oxidation of the peroxidase probe ABTS to ABTS cation radical (ABTS(•+)) has been studied. Both sulfinates are able to inhibit the oxidation of ABTS mediated by CO3(•-). The effect of hypotaurine and cysteine sulfinic acid against SOD inactivation by H2O2 (~42% protection of enzyme activity) has also been investigated. Interestingly, hypotaurine and cysteine sulfinic acid partially avoid the H2O2-mediated SOD inactivation, suggesting that the two sulfinates may have access to the SOD reactive site and preserve it by reacting with the copper-bound oxidant. In this way hypotaurine and cysteine sulfinic acid not only intercept CO3(•-) which could move out from the reactive site and cause oxidative damage, but also prevents the inactivation of SOD. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 10 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 3 | 30% |
Professor > Associate Professor | 2 | 20% |
Student > Bachelor | 2 | 20% |
Student > Doctoral Student | 1 | 10% |
Unknown | 2 | 20% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 4 | 40% |
Chemistry | 3 | 30% |
Neuroscience | 1 | 10% |
Unknown | 2 | 20% |