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Results: 5

1.
FIG. 3.

FIG. 3. From: Generation by a Widely Applicable Approach of a Hybrid Dioxygenase Showing Improved Oxidation of Polychlorobiphenyls .

Time course of HOPDA formation. Absorbance (milliunits) at absorption maxima (mAmax) are shown. The substrates were 3,3′-CB (circles) and 2,5,4′-CB (squares). Both substrates were initially oxidized by BphA-B4h.

Beatriz Cámara, et al. Appl Environ Microbiol. 2007 April;73(8):2682-2689.
2.
FIG. 5.

FIG. 5. From: Generation by a Widely Applicable Approach of a Hybrid Dioxygenase Showing Improved Oxidation of Polychlorobiphenyls .

Bottlenecks in the metabolism of specific ortho,meta-dioxygenated chlorinated BDHDs by enzymes BphB, BphC, and BphD of the pathway from B. xenovorans LB400. Thin arrows symbolize low transformation; crossed-out thin arrows symbolize no detectable transformation.

Beatriz Cámara, et al. Appl Environ Microbiol. 2007 April;73(8):2682-2689.
3.
FIG. 1.

FIG. 1. From: Generation by a Widely Applicable Approach of a Hybrid Dioxygenase Showing Improved Oxidation of Polychlorobiphenyls .

Upper pathway for catabolism of biphenyls encoded by the bph locus of B. xenovorans LB400. Compounds: 1, biphenyl; 2, biphenyl-2,3-dihydro-2,3-diol (BDHD); 3, 2,3-dihydroxybiphenyl (DHB); 4, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA); 5a, 2-hydroxypenta-2,4-dienoic acid; 5b, benzoic acid. Enzymes: BphA, biphenyl 2,3-dioxygenase; BphB, 2,3-dihydro-2,3-dihydroxybiphenyl 2,3-dehydrogenase; BphC, 2,3-dihydroxybiphenyl 1,2-dioxygenase; BphD, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase.

Beatriz Cámara, et al. Appl Environ Microbiol. 2007 April;73(8):2682-2689.
4.
FIG. 4.

FIG. 4. From: Generation by a Widely Applicable Approach of a Hybrid Dioxygenase Showing Improved Oxidation of Polychlorobiphenyls .

Overview of the regiospecificity of CB dioxygenation by BphA-B4h and -LB400. Regiospecificities of attack are symbolized by O2 molecules with arrows. Relative quantities are indicated as follows: black arrows, >33% of total dioxygenation; gray arrows, 10 to 33% of total dioxygenation; light gray arrows, <10% of total dioxygenation. For experimental evidence of site assignments and further details, see the text and Table 1. A lack of experimental evidence for the assignment of an oxidation site is indicated by “S?”; a lack of experimental evidence for the assignment of the relative quantity of oxidation is indicated by “Q?”

Beatriz Cámara, et al. Appl Environ Microbiol. 2007 April;73(8):2682-2689.
5.
FIG. 2.

FIG. 2. From: Generation by a Widely Applicable Approach of a Hybrid Dioxygenase Showing Improved Oxidation of Polychlorobiphenyls .

Generation of the fusion dioxygenase. The top line shows a representation of the bphA gene cluster of B. xenovorans LB400, encoding alpha and beta subunits (bphA1/bphA2), ferredoxin (bphA3), and ferredoxin reductase (bphA4). The hatched bphA1 segment between the restriction sites was exchanged with a PCR amplicon. The bottom line shows a representation of the alpha subunit. Catalytic and Rieske domains are shown in gray or are hatched, respectively. Horizontally connected vertical bars indicate sites encoding amino acid ligands of the Rieske iron-sulfur cluster ([2Fe-2S]) and of the active site mononuclear iron (mono-Fe). The part encoded by the amplicon and the flanking amino acid positions of the recipient subunit are indicated.

Beatriz Cámara, et al. Appl Environ Microbiol. 2007 April;73(8):2682-2689.

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