ArticleBiochemistry2009
Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysis.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 64 citations in OpenAlex.
- The curious life of human mitochondrial SOD2.International journal of biological macromolecules · 2026Review
- Manganese Superoxide Dismutase: Structure, Function, and Implications in Human Disease.Antioxidants (Basel, Switzerland) · 2025Review
- SOD2 is a regulator of proteasomal degradation promoting an adaptive cellular starvation response.Cell reports · 2025Article
- A lesson in symmetry.Nature structural & molecular biology · 2024Article
- MnSOD Mimetics in Therapy: Exploring Their Role in Combating Oxidative Stress-Related Diseases.Antioxidants (Basel, Switzerland) · 2024Review
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.Nature communications · 2024Article
- The role of Tyr34 in proton-coupled electron transfer of human manganese superoxide dismutase.Research square · 2024Article
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.Research square · 2024Article
- Perfect Crystals: microgravity capillary counterdiffusion crystallization of human manganese superoxide dismutase for neutron crystallography.NPJ microgravity · 2023Article
- Determination of Manganese in Serum Using GFAAS: Serum Reference Values for Manganese in the Adolescent Girls of the DERVAN Cohort.Indian journal of clinical biochemistry : IJCB · 2022Article
- Cobinamide is a strong and versatile antioxidant that overcomes oxidative stress in cells, flies, and diabetic mice.PNAS nexus · 2022Article
- The structure-function relationships and physiological roles of MnSOD mutants.Bioscience reports · 2022Review
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase.Nature communications · 2021Article
- Effects of dietary plant polyphenols and seaweed extract mixture on male-rabbit semen: Quality traits and antioxidant markers.Saudi journal of biological sciences · 2021Article
- Combined QM/MM and Monte Carlo study for redox leveling in Mn and Fe superoxide dismutase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- A Review of the Catalytic Mechanism of Human Manganese Superoxide Dismutase.Antioxidants (Basel, Switzerland) · 2018Review
- Insights into the Dichotomous Regulation of SOD2 in Cancer.Antioxidants (Basel, Switzerland) · 2017Review
- Substrate-analog binding and electrostatic surfaces of human manganese superoxide dismutase.Journal of structural biology · 2017Article
- LC-MS/MS Analysis Unravels Deep Oxidation of Manganese Superoxide Dismutase in Kidney Cancer.International journal of molecular sciences · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Superoxide dismutase (SOD) enzymes are critical in controlling levels of reactive oxygen species (ROS) that are linked to aging, cancer, and neurodegenerative disease. Superoxide (O(2)(*-)) produced during respiration is removed by the product of the SOD2 gene, the homotetrameric manganese superoxide dismutase (MnSOD). Here, we examine the structural and catalytic roles of the highly conserved active-site residue Tyr34, based upon structure-function studies of MnSOD enzymes with mutations at this site. Substitution of Tyr34 with five different amino acids retained the active-site protein structure and assembly but caused a substantial decrease in the catalytic rate constant for the reduction of superoxide. The rate constant for formation of the product inhibition complex also decreases but to a much lesser extent, resulting in a net increase in the level of product inhibited form of the mutant enzymes. Comparisons of crystal structures and catalytic rates also suggest that one mutation, Y34V, interrupts the hydrogen-bonded network, which is associated with a rapid dissociation of the product-inhibited complex. Notably, with three of the Tyr34 mutants, we also observe an intermediate in catalysis, which has not been reported previously. Thus, these mutants establish a means of trapping a catalytic intermediate that promises to help elucidate the mechanism of catalysis.
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Registered trials
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