The kinetic investigations of oxidation of tris(1,10-phenanthroline)iron(II) by oxone have been studied spectrophotometrically in phosphate buffer medium of pH 6.8, temperature 3081<, and ionic strength 0.25 mol L-1. The reactions were also carried out in presence of globular transport protein, bovine serum albumin (BSA) having isoelectric point 4.9, anionic surfactant sodium dodecyl sulfate (SDS), and their mixtures. The critical aggregation concentration (CAC) and critical micelle concentration (CMC) of SDS in presence of BSA have been determined using conductivity and kinetic measurement techniques. The secondary structure of BSA was examined by Circular Dichroism (CD) measurement at 308 K. The helix nature of BSA decreases with increase of SDS concentration. The effect of pH on rate in presence of BSA is opposite to its absence, and the effect of urea on rate in presence of BSA indicates the denaturation of BSA. The results depict that amphiphile SDS interacts with BSA and different molecular events, for example, specific binding, cooperative binding, protein unfolding, and micelle formation act. Activation parameters of the reaction in different environments have been determined. (C) 2012 Elsevier Inc. All rights reserved.