Human Mn-superoxide dismutase inactivation by peroxynitrite: a paradigm of metal-catalyzed tyrosine nitration in vitro and in vivo-Reference-Cited by-同舟云学术

Human Mn-superoxide dismutase inactivation by peroxynitrite: a paradigm of metal-catalyzed tyrosine nitration in vitro and in vivo

Published:2018 Issue:5 Volume:10 Page:679-695
ISSN:1756-5901
Container-title:Metallomics
language:en
Short-container-title:Metallomics

Author:

Demicheli Verónica¹²³⁴⁵,Moreno Diego M.⁶⁷⁸⁹¹⁰,Radi Rafael¹²³⁴⁵^ORCID

Affiliation:

1. Departmento de Bioquimica

2. Facultad de Medicina

3. Center for Free Radical and Biomedical Research

4. Universidad de la República

5. Montevideo

6. Instituto de Química Rosario (IQUIR, CONICET-UNR)

7. Área Química General e Inorgánica

8. Facultad de Ciencias Bioquímicas y Farmacéuticas

9. Universidad Nacional de Rosario

10. Argentina

Abstract

Nitration of human MnSOD at active site Tyr34 represents a biologically-relevant oxidative post-translational modification that causes enzyme inactivation.

Funder

Universidad de la República Uruguay

Publisher

Oxford University Press (OUP)

Subject

Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2018/MT/C7MT00348J

Reference167 articles.

1. Haemocuprein and hepatocuprein, copper-protein compounds of blood and liver in mammals

2. An Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase

3. Superoxide Dismutases and Superoxide Reductases

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