Experimental and theoretical structural/spectroscopical correlation of enterobactin and catecholamide

Area of Science:

• Computational chemistry
• Spectroscopy
• Biophysical chemistry

Background:

• Enterobactin is a siderophore crucial for iron uptake in bacteria.
• Understanding the structure and reactivity of iron-enterobactin complexes is vital for biological and chemical applications.

Purpose of the Study:

• To computationally determine IR spectra of iron-enterobactin in catecholate conformations.
• To correlate these theoretical spectra with experimental data.
• To investigate the structural dynamics and electronic properties of enterobactin.

Main Methods:

• Density Functional Theory (DFT) calculations (PBE/QZVP) for IR spectra.
• Matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) mass spectrometry for fragmentation analysis.
• Molecular Dynamics (MD) simulations to study dihedral angle distributions.

Main Results:

• IR spectra of [CatFeEB]^3- were calculated and correlated with experimental [SalH₃FeEB]⁰.
• MALDI-TOF MS elucidated fragments of FeEnterobactin and Enterobactin (H₆EB).
• Dependence of frontier orbitals (HOMO/LUMO) on dihedral angles of H₆EB was reported.

Conclusions:

• The study provides a comprehensive understanding of iron-enterobactin's spectral properties.
• Molecular dynamics and computational methods enhance the knowledge of H₆EB's structural dynamics and reactivity.
• This work bridges theoretical calculations and experimental observations for iron-enterobactin.