ArticleThe Journal of biological chemistry2015
Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
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- Hemoglobin in Submicron Particles (HbMPs) Is Stabilized Against Oxidation.Antioxidants (Basel, Switzerland) · 2024Article
- Insights into Molecular Mechanisms of Anticancer Activity ofPlants (Basel, Switzerland) · 2024Article
- Chemical Composition, Antioxidant Activities, Antidepressant Effect, and Lipid Peroxidation of Peruvian Blueberry: Molecular Docking Studies on Targets Involved in Oxidative Stress and Depression.Plants (Basel, Switzerland) · 2024Article
- Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond.The Journal of biological chemistry · 2023Article
- Characterization of a Novel Superoxide Dismutase from a Deep-sea Sea Cucumber (Antioxidants (Basel, Switzerland) · 2023Article
- Purple Sweet Potato Powder Containing Anthocyanin Mitigates High-Fat-Diet-Induced Dry Eye Disease.International journal of molecular sciences · 2023Article
- Serum zinc deficiency could be associated with dementia conversion in Parkinson's disease.Frontiers in aging neuroscience · 2023Article
- Relative Bioavailability of Broiler Chickens Fed with Zinc Hydroxychloride and Sulfate Sources for Corn-Soybean Meal.Biological trace element research · 2022Article
- SOD1 in ALS: Taking Stock in Pathogenic Mechanisms and the Role of Glial and Muscle Cells.Antioxidants (Basel, Switzerland) · 2022Review
- Biochemical Analysis ofACS infectious diseases · 2022Article
- Review
- Nitric oxide inhibits endothelial cell apoptosis by inhibiting cysteine-dependent SOD1 monomerization.FEBS open bio · 2022Article
- First Principles Calculation of Protein-Protein Dimer Affinities of ALS-Associated SOD1 Mutants.Frontiers in molecular biosciences · 2022Article
- Tripartite Separation of Glomerular Cell Types and Proteomes from Reporter-Free Mice.Journal of the American Society of Nephrology : JASN · 2021Article
- Phenotypic diversity in ALS and the role of poly-conformational protein misfolding.Acta neuropathologica · 2021Review
- Antioxidant Resveratrol Increases Lipolytic and Reduces Lipogenic Gene Expression under In Vitro Heat Stress Conditions in Dedifferentiated Adipocyte-Derived Progeny Cells from Dairy Cows.Antioxidants (Basel, Switzerland) · 2021Article
- Multiple ways to a dead end: diverse mechanisms by which ALS mutant genes induce cell death.Cell cycle (Georgetown, Tex.) · 2021Review
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Authors and funding
13 authors.
Funding
Abstract
The functional and structural significance of the intrasubunit disulfide bond in copper-zinc superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1 (hSOD) and yeast SOD1 lacking the disulfide bond. We determined x-ray crystal structures of metal-bound and metal-deficient hC57S SOD1. C57S hSOD1 isolated from yeast contained four zinc ions per protein dimer and was structurally very similar to wild type. The addition of copper to this four-zinc protein gave properly reconstituted 2Cu,2Zn C57S hSOD, and its spectroscopic properties indicated that the coordination geometry of the copper was remarkably similar to that of holo wild type hSOD1. In contrast, the addition of copper and zinc ions to apo C57S human SOD1 failed to give proper reconstitution. Using pulse radiolysis, we determined SOD activities of yeast and human SOD1s lacking disulfide bonds and found that they were enzymatically active at ∼10% of the wild type rate. These results are contrary to earlier reports that the intrasubunit disulfide bonds in SOD1 are essential for SOD activity. Kinetic studies revealed further that the yeast mutant SOD1 had less ionic attraction for superoxide, possibly explaining the lower rates. Saccharomyces cerevisiae cells lacking the sod1 gene do not grow aerobically in the absence of lysine, but expression of C57S SOD1 increased growth to 30-50% of the growth of cells expressing wild type SOD1, supporting that C57S SOD1 retained a significant amount of activity.
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