This work describes the formation and possible electrochemical application of a novel nanocomposite based on single-walled carbon nanotubes (SWNTs) and imidazolium-based room-temperature ionic liquids (RTILs) of 1-butyl-3-methylimidazolium tetrafluoroborate (Lbmim]BF4, ahydrophilic RTIL) and 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim]PF6, ahydrophobic RTIL). The nanocomposites ([bmim]BF4-SWNTs, and [bmim]PF6-SWNTs) were formed by simply grinding the SWNTs with the respective RTIL. The results of the X-ray photoelectron spectroscopy (XPS) and Raman spectroscopy indicated that the nanocomposites were formed by adsorption of an imidazolium ion on the surface of SWNTs via the "cation-pi" interaction. SEM images showed that [bmim]BF4-SWNTs (or [bmim]PF6-SWNTs) nanocomposites could uniformly cover the surface of a glassy carbon (GQ electrode resulting in a RTILs-SWNTs/GC modified electrode with a high stability. The RTlLs-SWNTs composite could be readily used as a matrix to immobilize heme-containing proteins/enzymes (myoglobin, cytochrome c, and horseradish peroxidase) without undergoing denaturation, as was verified by UV-vis and circular dichroic (CD) spectroscopic results. The voltammetric results showed that heme-containing proteins/enzymes entrapped in RTILs-SWNTs composites displayed a pair of well-defined, stable redox peaks, which were ascribed to their direct electron-transfer reactions. The results of controlled experiments showed that the positive charged imidazolium ion played a significant effect on the electrochemical parameters, such as the redox peak separation and the value of the formal potentials, etc., of the electron-transfer reaction of non-neutral species dissolved in solution or immobilized on the electrode surface. Further results demonstrated that the heme-containing proteins/enzymes entrapped in RTlLs-SWNTs composites could still retain their bioelectrocatalytic activity toward the reduction of oxygen and hydrogen peroxide. The results depicted in this work may pave a new avenue to electrocatalysis, proteins/enzymes electrochemistry, and bioelectrochemical synthesis, etc. (c) 2007 Elsevier Ltd. All rights reserved.