Copper Sources for Sod1 Activation.

Stefanie D. Boyd,Duane D. Winkler,Amelie Skopp,Morgan S. Ullrich

doi:10.3390/antiox9060500

Stefanie D. Boyd, Duane D. Winkler + Show 2 more

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https://doi.org/10.3390/antiox9060500

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Journal: Antioxidants	Publication Date: Jun 7, 2020
Citations: 24	License type: CC BY 4.0

Affiliation: The University of Texas at Dallas

Abstract

Copper ions (i.e., copper) are a critical part of several cellular processes, but tight regulation of copper levels and trafficking are required to keep the cell protected from this highly reactive transition metal. Cu, Zn superoxide dismutase (Sod1) protects the cell from the accumulation of radical oxygen species by way of the redox cycling activity of copper in its catalytic center. Multiple posttranslational modification events, including copper incorporation, are reliant on the copper chaperone for Sod1 (Ccs). The high-affinity copper uptake protein (Ctr1) is the main entry point of copper into eukaryotic cells and can directly supply copper to Ccs along with other known intracellular chaperones and trafficking molecules. This review explores the routes of copper delivery that are utilized to activate Sod1 and the usefulness and necessity of each.

Highlights

Numerous cellular processes cannot function without intracellular copper working in the active site of enzymes
Copper is tightly regulated due to the vital roles it plays within the cell, and because of its potential for adverse redox activity [2]
Copper’s journey in the mammalian cell begins when it is imported by Ctr1 [26]

Summary

Introduction

Numerous cellular processes cannot function without intracellular copper working in the active site of enzymes. Zn superoxide dismutase (Sod1) is an antioxidant enzyme that eliminates superoxide anions (O2 − ) from within the cell as a method of heading off the production of the more dangerous hydroxyl radicals (·OH) [4,5]. The key to copper’s broad utility arises from its ability to cycle between two oxidative states: Cu(I) and Cu(II) [9]. This redox property of copper allows it to function as both an electron donor and recipient, this can lead to the nonenzymatic production of hydroxyl radicals from the breakdown of hydrogen peroxide (H2 O2 ) [2,9,10]. Forms of Sod can be substituted between species without any phenotypic change to the organisms [11,12,13,14]

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