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Purification and Properties of p-Hydroxybenzoate Hydroxylases from Rhodococcus Strains

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Abstract

Gram-positive bacteria of the genus Rhodococcus catabolize p-hydroxybenzoate (PHB) through the initial formation of 3,4-dihydroxybenzoate. High levels of p-hydroxybenzoate hydroxylase (PHBH) activity are induced in six different Rhodococcus species when these strains are grown on PHB as sole carbon source. The PHBH enzymes were purified to apparent homogeneity and appeared to be homodimers of about 95 kD with each subunit containing a relatively weakly bound FAD. In contrast to their counterparts from gram-negative microorganisms, the Rhodococcus PHBH enzymes prefer NADH to NADPH as external electron donor. All purified enzymes were inhibited by Cl– and for five of six enzymes more pronounced substrate inhibition was observed in the presence of chloride ions.

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Authors and Affiliations

  1. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, Russia

    A. P. Jadan, L. A. Golovleva & E. L. Golovlev

  2. Laboratory of Biochemistry, Department of Agrotechnology and Food Sciences, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, Netherlands

    A. P. Jadan & W. J. H. van Berkel

Authors
  1. A. P. Jadan
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  2. W. J. H. van Berkel
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  3. L. A. Golovleva
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  4. E. L. Golovlev
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Jadan, A.P., van Berkel, W.J.H., Golovleva, L.A. et al. Purification and Properties of p-Hydroxybenzoate Hydroxylases from Rhodococcus Strains. Biochemistry (Moscow) 66, 898–903 (2001). https://doi.org/10.1023/A:1011908920472

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