title: Probing the interaction of mutiwalled carbon nanotubes and catalase: mutispectroscopic approach.
abstract: In this study, the mechanism of the interaction between multiwalled carbon nanotubes (MWCNTs) and catalase was investigated by fluorescence, UV-vis, and circular dichroism (CD) spectroscopy under physiological conditions. The fluorescence quenching mechanism of catalase by MWCNTs was shown to be a static quenching procedure and was a result of the formation of a catalase-MWCNT complex. The secondary structure and conformation of the catalase adsorbed on MWCNTs was determined by CD and UV-vis spectroscopy, and the results indicate that the catalase in this complex is partially unfolded with its lost in α-helical content and obtainment in β-sheet content. Moreover, binding of MWCNTs to catalase inhibited the enzymatic activity, which may trigger some toxic effects and undesirable physiological consequences.
authors.affiliation: Department of Plant Science, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai, 200240, People's Republic of China.
authors.forename: Meihong
authors.initials: M
authors.lastname: Xu
authors.forename: Zhonghua
authors.initials: Z
authors.lastname: Sheng
authors.forename: Wenyu
authors.initials: W
authors.lastname: Lu
authors.forename: Tianchun
authors.initials: T
authors.lastname: Dai
authors.forename: Cailing
authors.initials: C
authors.lastname: Hou
mesh_terms: D000327:Adsorption; D002374:Catalase / Q000737:chemistry*; D002942:Circular Dichroism; D037742:Nanotubes, Carbon / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
chemical_list: D037742:Nanotubes, Carbon; D002374:Catalase