Structure of Protocatechuate 3,4-Dioxygenase from Pseudomonas aeruginosa at 2.15 Å Resolution

Ohlendorf, D.H.; Orville, Allen M.; Lipscomb, John D.

doi:10.1006/jmbi.1994.1754

Cited by 185 publications

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“…These enzymes catalyze the cleavage of molecular oxygen accompanied by insertion of both oxygen atoms between the vicinal hydroxyl groups of the catecholic substrate, resulting in ring cleavage to yield muconic acid derivatives (3-5, 18, 19). The resting state of intradiol dioxygenases contains a highspin ferric center in a distorted trigonal bipyramidal geometry, with Tyr and His as the axial ligands and Tyr, His, and a hydroxide ligand defining the equatorial plane (20)(21)(22). Upon anaerobic substrate binding, the active site shifts to a square pyramidal geometry in which the axial Tyr and equatorial OH Ϫ are displaced by the substrate, which binds bidentate in its doubly deprotonated form (23,24).…”

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confidence: 99%

Substrate activation for O ₂ reactions by oxidized metal centers in biology

Pau

Lipscomb

Solomon

2007

Proc. Natl. Acad. Sci. U.S.A.

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The uncatalyzed reactions of O 2 (S = 1) with organic substrates (S = 0) are thermodynamically favorable but kinetically slow because they are spin-forbidden and the one-electron reduction potential of O 2 is unfavorable. In nature, many of these important O 2 reactions are catalyzed by metalloenzymes. In the case of mononuclear non-heme iron enzymes, either Fe II or Fe III can play the catalytic role in these spin-forbidden reactions. Whereas the ferrous enzymes activate O 2 directly for reaction, the ferric enzymes activate the substrate for O 2 attack. The enzyme–substrate complex of the ferric intradiol dioxygenases exhibits a low-energy catecholate to Fe III charge transfer transition that provides a mechanism by which both the Fe center and the catecholic substrate are activated for the reaction with O 2 . In this Perspective, we evaluate how the coupling between this experimentally observed charge transfer and the change in geometry and ligand field of the oxidized metal center along the reaction coordinate can overcome the spin-forbidden nature of the O 2 reaction.

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confidence: 99%

Substrate activation for O ₂ reactions by oxidized metal centers in biology

Pau

Lipscomb

Solomon

2007

Proc. Natl. Acad. Sci. U.S.A.

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“…[a15]n. Determination of the crystal structure of this enzyme from P. putida (formerly P. aeruginosa), showed that the iron atom is coordinated by four amino acids in the 15 subunit, and the active site is located at the interface between both subunits (26,27). X-ray analysis of C120 structure will clarify the geometry of the iron binding site.…”

Section: Vol 39 No 4 1996mentioning

confidence: 96%

“…On the contrary to the a subunit of C120, the ~ subunit of PC34D has been reported to contain vestigial iron binding site (26,27). And it has been suggested that the ancestor of PC34D was a homodimer with two active sites.…”

Section: Vol 39 No 4 1996mentioning

confidence: 99%

“…After a gene duplication, the polypeptide diverged to allow the formation of aggregates to enhance its stability (26,27). Contrary to PC34D whose genes locate at a neighboring position, it is likely that catA~ duplicated at another place on the chromosome which is far apart from the original position, and developed into another gene, catAa, with a conserved sequence which is essential for enzyme activity, and caused the unique subunit assembly to produce three isozymes.…”

Section: Biochemistry and Molecular Biology Internationalmentioning

confidence: 99%

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Amino acid sequence of catechol 1,2‐dioxygenase (pyrocatechase) isozyme αα from Pseudomonas arvilla C‐1

et al. 1996

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SummaryCatechol 1,2-dioxygenase catalyzes the oxygenative ring cleavage of catechol to form cis, cis-muconic acid, and contains a ferric form of iron as its sole cofactor. Pseudomonas arvilla C-1 contains three isozymes of the enzyme, a•, cz [3, and [3[3 [C. Nakai et al. (1990) Biol. Chem. 265, 660-665]. We have determined the amino acid sequence of the aa isozyme by direct analysis. The sequence shared 77% homology with isozyme N3, and had conserved tyrosyl and histidyl residues which are thought to be involved in the binding of ferric ion.

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“…5) The protocatechuate branch of the β-ketoadipate pathway begins with an ortho-cleavage of 1 by PcaHG, a protocatechuate 3,4-dioxygenase ( Fig. 1), 6,7) resulting in the formation of 3. PcaB, a 3-carboxy-cis,cis-muconate cycloisomerase, catalyzes the lactonization of 3 to form 4.…”

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In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL: the protocatechuate branch of the β-ketoadipate pathway in Rhodococcus jostii RHA1

Yamanashi

Kim

Hara

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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The β-ketoadipate pathway is a major pathway involved in the catabolism of the aromatic compounds in microbes. The recent progress in genome sequencing has led to a rapid accumulation of genes from the β-ketoadipate pathway in the available genetic database, yet the functions of these genes remain uncharacterized. In this study, the protocatechuate branch of the β-ketoadipate pathway of Rhodococcus jostii was reconstituted in vitro. Analysis of the reaction products of PcaHG, PcaB, and PcaL was achieved by high-performance liquid chromatography. These reaction products, β-ketoadipate enol-lactone, 3-carboxy-cis,cis-muconate, γ-carboxymuconolactone, muconolactone, and β-ketoadipate, were further characterized using LC-MS and nuclear magnetic resonance. In addition, the in vitro reaction of PcaL, a bidomain protein consisting of γ-carboxy-muconolactone decarboxylase and β-ketoadipate enol-lactone hydrolase activities, was demonstrated for the first time. This work provides a basis for analyzing the catalytic properties of enzymes involved in the growing number of β-ketoadipate pathways deposited in the genetic database.

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Structure of Protocatechuate 3,4-Dioxygenase from Pseudomonas aeruginosa at 2.15 Å Resolution

Cited by 185 publications

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Substrate activation for O ₂ reactions by oxidized metal centers in biology

Substrate activation for O ₂ reactions by oxidized metal centers in biology

Amino acid sequence of catechol 1,2‐dioxygenase (pyrocatechase) isozyme αα from Pseudomonas arvilla C‐1

In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL: the protocatechuate branch of the β-ketoadipate pathway in Rhodococcus jostii RHA1

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Structure of Protocatechuate 3,4-Dioxygenase from Pseudomonas aeruginosa at 2.15 Å Resolution

Cited by 185 publications

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Substrate activation for O 2 reactions by oxidized metal centers in biology

Substrate activation for O 2 reactions by oxidized metal centers in biology

Amino acid sequence of catechol 1,2‐dioxygenase (pyrocatechase) isozyme αα from Pseudomonas arvilla C‐1

In vitro reconstitution of the catabolic reactions catalyzed by PcaHG, PcaB, and PcaL: the protocatechuate branch of the β-ketoadipate pathway in Rhodococcus jostii RHA1

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Substrate activation for O ₂ reactions by oxidized metal centers in biology

Substrate activation for O ₂ reactions by oxidized metal centers in biology