Table of Contents Author Guidelines Submit a Manuscript
Spectroscopy: An International Journal
Volume 27, Article ID 192591, 12 pages

Multispectroscopic Study of the Interaction of Chloramphenicol with Human Neuroglobin

Shandong Provincial Key Laboratory of Chemical Energy Storage and Novel Cell Technology, School of Chemistry and Chemical Engineering, Liaocheng University, Liaocheng 252059, China

Copyright © 2012 Lei Huang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The interaction between chloramphenicol (CHL) and neuroglobin (Ngb) has been investigated by using fluorescence, synchronous fluorescence, UV-Vis and circular dichroism (CD) spectroscopy. It has been found that CHL molecule can quench the intrinsic fluorescence of Ngb in a way of dynamic quenching mechanism, which was supported by UV-Vis spectral data. Their effective quenching constants ( 𝐾 S V ) are 2 . 2 × 1 0 4 , 2 . 6 × 1 0 4 , a n d 3 . 1 × 1 0 4  L·mol−1 at 298 K, 303 K, and 308 K, respectively. The enthalpy change ( Δ 𝐻 ) and entropy change ( Δ 𝑆 ) for this reaction are 26.42 kJ·mol−1 and 171.7 J·K−1, respectively. It means that the hydrophobic interaction is the main intermolecular force of the interaction between CHL and Ngb. Synchronous fluorescence spectra showed that the microenvironment of tryptophan and tyrosine residues of Ngb has been changed slightly. The fluorescence quenching efficiency of CHL to tyrosine residues is a little bit more than that to tryptophan residues of Ngb. Furthermore, CD spectra indicated that CHL can induce the formation of α-helix of Ngb.