Academic Journal
Hydroquinone dioxygenase from Pseudomonas fluorescens ACB:a novel member of the family of nonheme-iron(II)-dependent dioxygenases
| العنوان: | Hydroquinone dioxygenase from Pseudomonas fluorescens ACB:a novel member of the family of nonheme-iron(II)-dependent dioxygenases |
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| المؤلفون: | Moonen, Marielle J. H., Synowsky, Silvia A., van den Berg, Willy A. M., Westphal, Adrie H., Heck, Albert J. R., van den Heuvel, Robert H. H., Fraaije, Marco W., van Berkel, Willem J. H. |
| المصدر: | Moonen , M J H , Synowsky , S A , van den Berg , W A M , Westphal , A H , Heck , A J R , van den Heuvel , R H H , Fraaije , M W & van Berkel , W J H 2008 , ' Hydroquinone dioxygenase from Pseudomonas fluorescens ACB : a novel member of the family of nonheme-iron(II)-dependent dioxygenases ' , Journal of Bacteriology , vol. 190 , no. 15 , pp. 5199-5209 . https://doi.org/10.1128/JB.01945-07 |
| سنة النشر: | 2008 |
| المجموعة: | University of Groningen research database |
| مصطلحات موضوعية: | 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-DIOXYGENASE |
| الوصف: | 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. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| Relation: | https://research.rug.nl/en/publications/51c27874-9173-48f6-8688-894cf5f920e2 |
| DOI: | 10.1128/JB.01945-07 |
| الاتاحة: | https://hdl.handle.net/11370/51c27874-9173-48f6-8688-894cf5f920e2 https://research.rug.nl/en/publications/51c27874-9173-48f6-8688-894cf5f920e2 https://doi.org/10.1128/JB.01945-07 https://pure.rug.nl/ws/files/6721201/2008JBacteriolMoonen2.pdf |
| Rights: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.514B6C59 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1128/JB.01945-07 |
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