In this study, cphC-I and cphB, encoding a putative two-component flavin-diffusible monooxygenase (TC-FDM) complex, were cloned from Arthrobacter chlorophenolicus A6. The corresponding enzymes were overexpressed to assess the feasibility of their utilization for the oxidative decomposition of 4-chlorophenol (4-CP). Soluble CphC-I was produced at a high level (similar to 50%), and subsequently purified. Since CphB was expressed in an insoluble form, a flavin reductase, Fre, cloned from Escherichia coli was used as an alternative reductase. CphC-I utilized cofactor FADH(2), which was reduced by Fre for the hydroxylation of 4-CP. This recombinant enzyme complex exhibited a higher specific activity for the oxidation of 4-CP (45.34 U/mg-protein) than that exhibited by CphC-I contained in cells (0.18 U/mg-protein). The Michaelis-Menten kinetic parameters were determined as: v(max) = 223.3 mu M .min(-1), K-M = 249.4 lM, and k(cat)/K-M = 0.052 min(-1).mu M-1. These results could be useful for the development of a new biochemical remediation technique based on enzymatic agents catalyzing the degradation of phenolic contaminants. (C) 2017 Elsevier Ltd. All rights reserved.