Characterization of tetrachlorohydroquinone reductive dehalogenase from Sphingomonas sp. UG30

• Published in: Biochemical and biophysical research communications 2002-12, Vol.299 (4), p.634-640
• Main Authors: Habash, M.B, Beaudette, L.A, Cassidy, M.B, Leung, K.T, Hoang, T.A, Vogel, H.J, Trevors, J.T, Lee, H
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Cloning, Molecular; Humans; Hydrogen-Ion Concentration; Hydrolases - chemistry; Hydrolases - genetics; Hydrolases - metabolism; Hydroquinones - chemistry; Hydroquinones - metabolism; Molecular Sequence Data; Sequence Alignment; Sphingomonas - enzymology; Sphingomonas - genetics; Temperature
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(02)02711-0

Tetrachlorohydroquinone reductive dehalogenase (PcpC) is the second of three enzymes that catalyze the initial degradation of pentachlorophenol in Sphingomonas sp. UG30 and several other bacterial strains. The UG30 PcpC shares a high degree (94%) of primary sequence identity with the well-studied PcpC from Sphingobium chlorophenolicum ATCC 39723. Significant differences, however, were observed between the two PcpC enzymes in some of their functional and kinetic properties. The temperature optimum of the UG30 PcpC is 10 °C higher and the pH optimum is approximately 2 units higher than the S. chlorophenolicum PcpC. In addition, the S. chlorophenolicum PcpC is subject to inhibition by the substrate tetrachlorohydroquinone (TCHQ), and this has necessitated the use of a mutant enzyme, which was not inhibited by TCHQ, for kinetic studies. In contrast, the UG30 PcpC was not inhibited by TCHQ and this may allow detailed kinetic and mechanistic studies using the wild-type enzyme.