ArticleScientific reports2023
A novel hybrid protein composed of superoxide-dismutase-active Cu(II) complex and lysozyme.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 13 citations in OpenAlex.
- Crystal structure and Hirshfeld surface analysis of aqua-(1Acta crystallographica. Section E, Crystallographic communications · 2025Article
- New Glycosalen-Manganese(III) Complexes and RCABiomimetics (Basel, Switzerland) · 2023Article
- Improvement of the SOD activity of the CuFrontiers in chemistry · 2023Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
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Abstract
A novel hybrid protein composed of a superoxide dismutase-active Cu(II) complex (CuST) and lysozyme (CuST@lysozyme) was prepared. The results of the spectroscopic and electrochemical analyses confirmed that CuST binds to lysozyme. We determined the crystal structure of CuST@lysozyme at 0.92 Å resolution, which revealed that the His15 imidazole group of lysozyme binds to the Cu(II) center of CuST in the equatorial position. In addition, CuST was fixed in position by the weak axial coordination of the Thr89 hydroxyl group and the hydrogen bond between the guanidinium group of the Arg14 residue and the hydroxyl group of CuST. Furthermore, the combination of CuST with lysozyme did not decrease the superoxide dismutase activity of CuST. Based on the spectral, electrochemical, structural studies, and quantum chemical calculations, an O
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