Characterization of a ring-hydroxylating dioxygenase from phenanthrene-degrading Sphingomonas sp. strain LH128 able to oxidize benz[a]anthracene
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- 作者：Luc Schuler ; Yves Jouanneau ; Sin¨¦ad M. N¨ª Chadhain ; Christine Meyer ; Maria Pouli ; Gerben J. Zylstra ; Pascal Hols and Spiros N. Agathos
- 关键词：Bioremediation ; Meta ; cleavage operon genes ; Indigo formation ; Rieske nonheme iron oxygenase
- 刊名：Applied Microbiology and Biotechnology
- 出版年：2009
- 出版时间：June, 2009
- 年：2009
- 卷：83
- 期：3
- 页码：465-475
- 全文大小：1.1 MB
文摘
Sphingomonas sp. strain LH128 was isolated from a polycyclic aromatic hydrocarbon (PAH)-contaminated soil using phenanthrene as the sole source of carbon and energy. A dioxygenase complex, phnA1fA2f, encoding the α and β subunit of a terminal dioxygenase responsible for the initial attack on PAHs, was identified and isolated from this strain. PhnA1f showed 98 % , 78 % , and 78 % identity to the α subunit of PAH dioxygenase from Novosphingobium aromaticivorans strain F199, Sphingomonas sp. strain CHY-1, and Sphingobium yanoikuyae strain B1, respectively. When overexpressed in Escherichia coli, PhnA1fA2f was able to oxidize low-molecular-weight PAHs, chlorinated biphenyls, dibenzo-p-dioxin, and the high-molecular-weight PAHs benz[a]anthracene, chrysene, and pyrene. The action of PhnA1fA2f on benz[a]anthracene produced two benz[a]anthracene dihydrodiols.