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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

  • Conference paper
Taurine 10

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 975))

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.

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Abbreviations

ABTS:

2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulphonic)

CA:

Cysteic acid

CO3 •– :

Carbonate anion radical

CSA:

Cysteine sulfinic acid

H2O2 :

Hydrogen peroxide

HCO3 − :

Bicarbonate

HTAU:

Hypotaurine

RSO2 − :

Sulfinates

RSO2 • :

Sulfonyl radicals

RSO3 − :

Sulfonates

SOD:

Cu–Zn superoxide dismutase

TAU:

Taurine

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Authors and Affiliations

  1. Dipartimento di Scienze Biochimiche, Sapienza Università di Roma, Piazzale Aldo Moro, Rome, Italy

    Alessia Baseggio Conrado, Simonetta Maina, Antonio Francioso, Luciana Mosca, Elisabetta Capuozzo & Mario Fontana

  2. Photobiology Unit, University of Dundee, Ninewells Hospital and School of Mecine, Dundee, DD1 9SY, UK

    Alessia Baseggio Conrado & Harry Moseley

Authors
  1. Alessia Baseggio Conrado
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  2. Simonetta Maina
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  3. Harry Moseley
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  4. Antonio Francioso
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  5. Luciana Mosca
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  6. Elisabetta Capuozzo
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  7. Mario Fontana
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Correspondence to Alessia Baseggio Conrado .

Editor information

Editors and Affiliations

  1. Department of Life Sciences, University of Seoul, Seoul, South Korea

    Dong-Hee Lee  & Ha Won Kim  & 

  2. College of Medicine, University of South Alabama, Mobile, Alabama, USA

    Stephen W. Schaffer

  3. Department of Developmental Neurobiology, NY State Institute for Basic Research in Developmental Disabilities, New York, USA

    Eunkyue Park

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Baseggio Conrado, A. et al. (2017). 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. In: Lee, DH., Schaffer, S.W., Park, E., Kim, H.W. (eds) Taurine 10. Advances in Experimental Medicine and Biology, vol 975. Springer, Dordrecht. https://doi.org/10.1007/978-94-024-1079-2_43

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