Phthalate Dioxygenase Reductase

Ludwig, Martha; Ballou, David P.; Noodleman, Louis

doi:10.1002/0470028637.met148

Cited by 2 publications

(2 citation statements)

References 58 publications

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“…The enzyme has K m 0.3 and 0.125 mM for phthalate and oxygen, respectively [3]. Of the two components, the structure of reductase component is resolved at 2 Å [18,62]. Based on recent biophysical and modeling studies it has been proposed that phthalate 4,5-dioxygensae has two planar rings of α 3 -α 3 arangement one above the other unlike other rieske dioxygenases that has α and β subunits [96].…”

Section: Phthalate Dioxygenasementioning

confidence: 99%

Bacterial degradation of phthalate isomers and their esters

Vamsee-Krishna

Phale

2008

Indian J Microbiol

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Phthalate isomers and their esters are used heavily in various industries. Excess use and leaching from the product pose them as major pollutants. These chemicals are toxic, teratogenic, mutagenic and carcinogenic in nature. Various aspects like toxicity, diversity in the aerobic bacterial degradation, enzymes and genetic organization of the metabolic pathways from various bacterial strains are reviewed here. Degradation of these esters proceeds by the action of esterases to form phthalate isomers, which are converted to dihydroxylated intermediates by specifi c and inducible phthalate isomer dioxygenases. Metabolic pathways of phthalate isomers converge at 3,4-dihydroxybenzoic acid, which undergoes either ortho-or meta-ring cleavage and subsequently metabolized to the central carbon pathway intermediates. The genes involved in the degradation are arranged in operons present either on plasmid or chromosome or both, and induced by specifi c phthalate isomer. Understanding metabolic pathways, diversity and their genetic regulation may help in constructing bacterial strains through genetic engineering approach for effective bioremediation and environmental clean up.

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Section: Phthalate Dioxygenasementioning

confidence: 99%

Bacterial degradation of phthalate isomers and their esters

Vamsee-Krishna

Phale

2008

Indian J Microbiol

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“…This effect stems from hydrogen bond competition with sulfur-to-iron charge transfer and an increase in the negative charge on the sulfur ligands (5,50). Although a direct correlation between the number of hydrogen bonds and absolute change in cluster redox potential is not always apparent, in at least one case, a large change in redox potential between two highly similar [2Fe-2S] clusters has been attributed to the relative flipping of one main-chain NH-S hydrogen bond between the two protein structures (98). Electrostatic interactions also play a role in tuning redox potential.…”

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confidence: 99%

Iron-Based Redox Switches in Biology

Outten

Theil

2009

Antioxidants & Redox Signaling

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By virtue of its unique electrochemical properties, iron makes an ideal redox active cofactor for many biologic processes. In addition to its important role in respiration, central metabolism, nitrogen fixation, and photosynthesis, iron also is used as a sensor of cellular redox status. Iron-based sensors incorporate Fe-S clusters, heme, and mononuclear iron sites to act as switches to control protein activity in response to changes in cellular redox balance. Here we provide an overview of iron-based redox sensor proteins, in both prokaryotes and eukaryotes, that have been characterized at the biochemical level. Although this review emphasizes redox sensors containing Fe-S clusters, proteins that use heme or novel iron sites also are discussed.

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Phthalate Dioxygenase Reductase

Cited by 2 publications

References 58 publications

Bacterial degradation of phthalate isomers and their esters

Bacterial degradation of phthalate isomers and their esters

Iron-Based Redox Switches in Biology

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