Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 371651
Title Hydroquinone dioxygenase from Pseudomonas fluorescens ACB: A novel member of the family of non-heme iron (II)-dependent dioxygenases
Author(s) Moonen, M.J.H.; Synowsky, S.A.; Berg, W.A.M. van den; Westphal, A.H.; Heck, A.J.R.; Heuvel, R.H.H. van den; Fraaije, M.W.; Berkel, W.J.H. van
Source Journal of Bacteriology 190 (2008). - ISSN 0021-9193 - p. 5199 - 5209.
Department(s) Biochemistry
Publication type Refereed Article in a scientific journal
Publication year 2008
Keyword(s) baeyer-villiger oxidation - of-flight instrument - hydroxyquinol 1,2-dioxygenase - crystal-structure - p-nitrophenol - 4-hydroxyacetophenone monooxygenase - protocatechuate 4,5-dioxygenase - 2-aminophenol 1,6-dioxygenase - chlorinated acetophenones - gentisate 1,2
Abstract Hydroquinone 1,2-dioxygenase (HQDO), an enzyme involved in the catabolism of 4-hydroxyacetophenone in Pseudomonas fluorescens ACB, was purified to apparent homogeneity. Ligandation with 4-hydroxybenzoate prevented the enzyme from irreversible inactivation. HQDO was activated by iron (H) ions and catalyzed the ring fission of a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes. HQDO was inactivated by 2,2'-dipyridyl, o-phenanthroline, and hydrogen peroxide and inhibited by phenolic compounds. The inhibition with 4-hydroxybenzoate (K-i = 14 mu M) was competitive with hydroquinone. Online size-exclusion chromatography mass spectrometry revealed that HQDO is an alpha 2 beta 2 heterotetramer of 112.4 kDa, which is composed of an alpha-subunit of 17.8 kDa and a beta-subunit of 38.3 kDa. Each beta-subunit binds one molecule of 4-hydroxybenzoate and one iron(II) ion. N-terminal sequencing and peptide mapping and sequencing based on matrix-assisted laser desorption ionization-two-stage time of flight analysis established that the HQDO subunits are encoded by neighboring open reading frames (hapC and hapD) of a gene cluster, implicated to be involved in 4-hydroxyacetophenone degradation. HQDO is a novel member of the family of nonheme-iron(II)-dependent dioxygenases. The enzyme shows insignificant sequence identity with known dioxygenases.
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