Structural Insights into the Dynamics of Water in SOD1 Catalysis and Drug Interactions.

ABSTRACT: Superoxide dismutase 1 (SOD1) is a crucial enzyme that protects cells from oxidative damage by converting superoxide radicals into H₂O₂ and O₂. This detoxification process, essential for cellular homeostasis, relies on a precisely orchestrated catalytic mechanism involving the copper cation, while the zinc cation contributes to the structural integrity of the enzyme. This study presents the 2.3 Å crystal structure of human SOD1 (PDB ID: 9IYK), revealing an assembly of six homodimers and twelve distinct active sites. The water molecules form a complex hydrogen-bonding network that drives proton transfer and sustains active site dynamics. Our structure also uncovers subtle conformational changes that highlight the intrinsic flexibility of SOD1, which is essen

SUBMITTER: Yapici I 

PROVIDER: S-EPMC12071975 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature