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Benvenuti, M., Briganti, F., Scozzafava, A., Golovleva, L., Travkin, V.M. and Mangani, S. (1999) Crystallization and preliminary crystallographic analysis of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E: A novel dioxygenase involved in the biodegradation of polychlorinated aromatic compounds. Acta Crystallographica Section D: Biological Crystallography, D55, 901-903. doi:10.1107/S0907444998017715

has been cited by the following article:

• TITLE: Biphenyl- and carvone-induced protein expression patterns in Rhodococcus sp. ACS

  AUTHORS: Jong-Shik Kim

  KEYWORDS: Polychlorinated Biphenyl (PCB); Carvone; Rhodococcus; Protein Expression

  JOURNAL NAME: Journal of Agricultural Chemistry and Environment, Vol.2 No.3, August 9, 2013

  ABSTRACT: Protein expression patterns in the polychlorinated biphenyl (PCB)-degrading Rhodococcussp. strain ACS were examined following growth on two substrates capable of inducing the enantioselective biotransformation of PCBs via different degradation pathways. Eleven inducible proteins were identified by SDS-PAGE and characterized by LC-MS/MS. Four of the peptides, a spore coat protein, an extracellular serine protease, a spoVP, and a molecular chaperonin from Bacillus subtilis, were identified as being unique to biphenyl-induced cells, whereas anextracellular serine protease from B. subtilis was identified as being unique to carvone-induced cells. None of the peptides identified had sequences that corresponded to known dioxygenases or other PCB-degrading enzymes of this Gram- positive bacterium, suggesting that the identified induced proteins may be involved in either PCB degradation or adaptive responses that protect cells from toxicity.