In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways.

Polissi, Alessandra; Harayama, Shigeaki

doi:10.1002/j.1460-2075.1993.tb06004.x

Cited by 69 publications

(49 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…YAA (AB008831); PKO1, Ralstonia pickettii PKO1 (U20258). made by Polissi and Harayama (1993). Therefore, the results in this study proved that the xylT product in Pseudomonas sp.…”

Section: Resultssupporting

confidence: 66%

“…Reactivation of catechol 2,3-dioxygenase by XylT C23O is inactivated by exposure to air or during the catalytic cycle, especially when substituted catechols, such as 3-and 4-methylcatechol, were used as substrates (Bartels et al, 1984;Polissi and Harayama, 1993;Cerdan et al, 1994). Inactivation of the enzyme is primarily caused by the oxidation of ferrous iron that is present at the active site of the enzyme, but ultimately the oxidized iron atom may be released from the enzyme (Wasserfallen, 1989;Kim et al, 2000;Kim et al, 2001).…”

Section: Resultsmentioning

confidence: 99%

“…The inactivation of C23O also occurs during catalytic turnover when the substrate analogues, such as alkyl-or chloro-catechols (Bartels et al, 1984;Cerdan et al, 1994). Polissi and Harayama (1993) reported that a mechanism exists in vivo that hinders the irreversible inactivation of C23O. Mutant cells of Pseudomonas putida that lack a xylT gene lost their ability to grow on p-xylene and p-toluate as *To whom correspondence should be addressed.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Chloroplast-type Ferredoxin Involved in Reactivation of Catechol 2,3-Dioxygenase from Pseudomonas sp.S-47

Park¹,

Chae²,

Kim³

et al. 2002

BMB Reports

View full text Add to dashboard Cite

Pseudomonas sp. S-47 is capable of degrading catechol and 4-chlorocatechol via the meta-cleavage pathway. XylTE products catalyze the dioxygenation of the aromatics. The xylT of the strain S-47 is located just upstream of the xylE gene. XylT is a typical chloroplast-type ferredoxin, which is characterized by 4 cystein residues that are located at positions 41, 46, 49, and 81. The chloroplast-type ferredoxin of Pseudomonas sp. S-47 exhibited a 98% identity with that of P. putida mt-2 (TOL plasmid) in the amino acid sequence, but only about a 40 to 60% identity with the corresponding enzymes from other organisms. We constructed two recombinant plasmids (pRES1 containing xylTE and pRES101 containing xylE without xylT) in order to examine the function of XylT for the reactivation of the catechol 2,3-dioxygenase (XylE) that is oxidized with hydrogen peroxide. The pRES1 that was treated with hydrogen peroxide was recovered in the catechol 2,3-dioxygenase (C23O) activity about 4 minutes after incubation, but the pRES101 showed no recovery. That means that the typical chloroplast-type ferredoxin (XylT) of Pseudomonas sp. S-47 is involved in the reactivation of the oxidized C23O in the dioxygenolytic cleavage of aromatic compounds.

show abstract

“…YAA (AB008831); PKO1, Ralstonia pickettii PKO1 (U20258). made by Polissi and Harayama (1993). Therefore, the results in this study proved that the xylT product in Pseudomonas sp.…”

Section: Resultssupporting

confidence: 66%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Chloroplast-type Ferredoxin Involved in Reactivation of Catechol 2,3-Dioxygenase from Pseudomonas sp.S-47

Park¹,

Chae²,

Kim³

et al. 2002

BMB Reports

View full text Add to dashboard Cite

show abstract

“…Interestingly, the partition ratio of catechol 2,3-dioxygenase for catechol is 1,400,000 (28), indicating that DHBD is much more susceptible than is catechol 2,3-dioxygenase to suicide inactivation by its putative preferred substrate. Despite the higher susceptibility of DHBD to suicide inactivation, the bph pathway apparently does not contain a homologue to XylT, the small ferredoxin of the TOL pathway, which serves to maintain the active site iron of catechol 2,3-dioxygenase in the ferrous state (34).…”

mentioning

confidence: 99%

Molecular Basis for the Stabilization and Inhibition of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase by t-Butanol

Vaillancourt

Han

Fortin

et al. 1998

Journal of Biological Chemistry

120

View full text Add to dashboard Cite

The steady-state cleavage of catechols by 2,3-dihydroxybiphenyl 1,2-dioxygenase (DHBD), the extradiol dioxygenase of the biphenyl biodegradation pathway, was investigated using a highly active, anaerobically purified preparation of enzyme. The kinetic data obtained using 2,3-dihydroxybiphenyl (DHB) fit a compulsory order ternary complex mechanism in which substrate inhibition occurs. The K m for dioxygen was 1280 ؎ 70 M, which is at least 2 orders of magnitude higher than that reported for catechol 2,3-dioxygenases. K m and K d for DHB were 22 ؎ 2 and 8 ؎ 1 M, respectively. DHBD was subject to reversible substrate inhibition and mechanism-based inactivation. In air-saturated buffer, the partition ratios of catecholic substrates substituted at C-3 were inversely related to their apparent specificity constants. Small organic molecules that stabilized DHBD most effectively also inhibited the cleavage reaction most strongly. The steady-state kinetic data and crystallographic results suggest that the stabilization and inhibition are due to specific interactions between the organic molecule and the active site of the enzyme. t-Butanol stabilized the enzyme and inhibited the cleavage of DHB in a mixed fashion, consistent with the distinct binding sites occupied by t-butanol in the crystal structures of the substrate-free form of the enzyme and the enzyme-DHB complex. In contrast, crystal structures of complexes with catechol and 3-methylcatechol revealed relationships between the binding of these smaller substrates and t-butanol that are consistent with the observed competitive inhibition.The microbial degradation of aromatic compounds constitutes an essential link in the global carbon cycle. The aerobic degradation of aromatic compounds such as toluene, naphthalene, and biphenyl generally proceeds via a catecholic catabolite with hydroxyl substituents on two adjacent carbon atoms. This catecholic compound is cleaved by a dioxygenase from one of two very different classes. Intradiol dioxygenases utilize non-heme ferric iron to cleave the aromatic nucleus ortho to (between) the hydroxyl substituents whereas extradiol dioxygenases utilize non-heme ferrous iron to cleave the aromatic nucleus meta (adjacent) to the hydroxyl substituents. The mechanism of intradiol dioxygenases is better understood due to their greater stability, favorable properties for spectroscopic examination, and the accessibility of catalytic intermediates (1, 2). Interest in extradiol dioxygenases is nonetheless considerable, not only because of their general metabolic significance and catalytic properties, but also because of the potential exploitation of these enzymes in the degradation of environmental pollutants such as polychlorinated biphenyls.2,3-Dihydroxybiphenyl 1,2-dioxygenase (DHBD) 1 is a component of the aerobic biphenyl degradation pathway of a number of microorganisms and cleaves 2,3-dihydroxybiphenyl (DHB) in an extradiol fashion as shown in Scheme 1. Crystallographic studies of DHBD from Burkholderia cepacia LB400 (3) and Pseudomonas...

show abstract

“…PhkR is homologous to DmpR 24) , suggesting that PhkR belongs to the NtrC family of transcriptional activators 16) as in the cases of the other phenol degraders. PhkG may be a ferredoxin-like protein having a similar function to XylT, which reactivates catechol 2,3-dioxygenase 22) . One incomplete ORF (designated phkH) was identified downstream of phkG.…”

Section: Nucleotide Sequence Of the Ph Genesmentioning

confidence: 99%

Characterization of the Phenol Hydroxylase from Burkholderia kururiensis KP23 Involved in Trichloroethylene Degradation by Gene Cloning and Disruption.

2003

View full text Add to dashboard Cite

Burkholderia kururiensis KP23 was isolated as a trichloroethylene (TCE)-degrading bacterium. Its degrading activity was induced by phenol, suggesting that the degradation is catalyzed by a phenol hydroxylase (PH). To elucidate the involvement of the PH in the degradation of TCE, the gene cluster for the enzyme was cloned and sequenced. The structural genes (phkABCDEFG) and cognate regulatory gene (phkR) were identified in a divergent transcriptional organization. The products are homologous to those of dmpRKLMNOPQ of Pseudomonas putida CF600, sharing 30-62% identity of amino acid sequence, indicating that the PH is a multi-component enzyme. Disruption of phkD encoding a large oxygenase subunit of the enzyme completely abolished the utilization of phenol as well as degradation of TCE by strain KP23. In addition, a disruptant of phkR was not able to grow on phenol and showed no activity to degrade TCE, indicating that PhkR is an activator and controls the expression of phkABCDEFG.

show abstract

In vivo reactivation of catechol 2,3-dioxygenase mediated by a chloroplast-type ferredoxin: a bacterial strategy to expand the substrate specificity of aromatic degradative pathways.

Cited by 69 publications

References 34 publications

Chloroplast-type Ferredoxin Involved in Reactivation of Catechol 2,3-Dioxygenase from Pseudomonas sp.S-47

Chloroplast-type Ferredoxin Involved in Reactivation of Catechol 2,3-Dioxygenase from Pseudomonas sp.S-47

Molecular Basis for the Stabilization and Inhibition of 2,3-Dihydroxybiphenyl 1,2-Dioxygenase by t-Butanol

Characterization of the Phenol Hydroxylase from Burkholderia kururiensis KP23 Involved in Trichloroethylene Degradation by Gene Cloning and Disruption.

Contact Info

Product

Resources

About