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An Interdisciplinary Study of Lysozyme Interactions with Hexacyanoferrate(III)/(II) Ions
Ola Grabowska1, Krzysztof Żamojć1, Anna Kloska2
1Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, Poland.
International Journal of Molecular Sciences
|September 13, 2025
Summary
Lysozyme binds hexacyanoferrate(III)/(II) ions via electrostatic and van der Waals forces, forming a 1:1 complex without affecting enzyme activity or bacterial cell viability.
Area of Science:
- Biochemistry
- Biophysics
- Computational Biology
Background:
- Lysozyme is a crucial enzyme in innate immunity.
- Hexacyanoferrate(III)/(II) ([Fe(CN)6]3-/4-) are redox-active inorganic ions.
Purpose of the Study:
- To characterize the binding interactions between lysozyme and hexacyanoferrate(III)/(II) ions.
- To investigate the impact of these interactions on lysozyme's structure, function, and biological activity.
Main Methods:
- Steady-state fluorescence spectroscopy (SF)
- Isothermal titration calorimetry (ITC)
- Circular dichroism spectroscopy (CD)
- Cyclic voltammetry (CV)
- Molecular dynamics simulations
Main Results:
- A 1:1 stoichiometric complex is formed between lysozyme and hexacyanoferrate(III)/(II) ions.
- Interactions are driven by electrostatic and van der Waals forces, enhancing electron transfer kinetics.
- Lysozyme's secondary structure and enzymatic activity remain unaffected.
- No interference with lysozyme's activity against Gram-positive and Gram-negative bacteria was observed.
Conclusions:
- Hexacyanoferrate(III)/(II) ions bind to specific surface regions of lysozyme.
- The binding does not compromise lysozyme's structural integrity or enzymatic function.
- [Fe(CN)6]3-/4- ions can be considered as potential modifiers of lysozyme activity without adverse effects.
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