• The catechol dioxygenases, some of the most well-studied dioxygenase enzymes, use dioxygen to cleave a carbon-carbon bond of an aromatic catechol ring system. (wikipedia.org)
  • A number of bacteria that can degrade a variety of aromatic compounds have been identified and the pathways involved in the degradation have been extensively characterized [ 3 , 4 ]. (biomedcentral.com)
  • In the convergent mode, structurally diverse aromatic compounds are converted to one of a few aromatic ring cleavage substrates such as catechol, gent sate, protocatechuate and their derivatives [ 5 ]. (biomedcentral.com)
  • For example, in the α-ketoglutarate-dependent enzymes, one atom of dioxygen is incorporated into two substrates, with one always being α-ketoglutarate, and this reaction is brought about by a mononuclear iron center. (wikipedia.org)
  • Oxygenases belong to the oxidoreductive group of enzymes (E.C. Class 1), which oxidize the substrates by transferring oxygen from molecular oxygen (O 2 ) and utilize FAD/NADH/NADPH as the co-substrate. (biomedcentral.com)
  • For instance, carbon-carbon bond cleavage, fatty acid hydroperoxidation, carbon-sulfur bond cleavage, and thiol oxidation are all reactions catalyzed by mononuclear iron dioxygenases. (wikipedia.org)
  • In this divergent mode, a metal-dependent dioxygenase channels these dihydroxylated intermediates into one of the two possible pathways: the meta -cleavage pathway or the ortho -cleavage pathway [ 7 - 9 ] (Fig. 1 ). (biomedcentral.com)
  • The mononuclear iron dioxygenases, or non-heme iron-dependent dioxygenases as they are also termed, all utilize a single catalytic iron to incorporate either one or both atoms of dioxygen into a substrate. (wikipedia.org)
  • Extradiol members utilize ferrous iron as the active redox state, and this center is commonly coordinated octahedrally through a 2-His-1-Glu motif with labile water ligands occupying empty positions. (wikipedia.org)
  • Dioxygenases are oxidoreductase enzymes. (wikipedia.org)
  • The most widely observed cofactor involved in dioxygenation reactions is iron, but the catalytic scheme employed by these iron-containing enzymes is highly diverse. (wikipedia.org)
  • Iron-containing dioxygenases can be subdivided into three classes on the basis of how iron is incorporated into the active site: those employing a mononuclear iron center, those containing a Rieske [2Fe-2S] cluster, and those utilizing a heme prosthetic group. (wikipedia.org)
  • Despite this common oxygenation event, the mononuclear iron dioxygenases are diverse in how dioxygen activation is used to promote certain chemical reactions. (wikipedia.org)
  • Advanced oxidation processes (APOs) of aromatic compounds, particularly of phenol, yield several benzene derivatives, such as hydroquinone, catechol, and resorcinol, as intermediate metabolites of its transformation. (hindawi.com)
  • Meanwhile, in the oxidative degradation of hydroquinone under a supercritical condition (409.9°C and 24.5 MPa) and subcritical condition (359.9°C and 24.5 MPa), -benzoquinone was to be an important intermediate [ 3 ]. (hindawi.com)
  • Once a catecholate substrate binds to the metal center in a bidentate fashion through the deprotonated hydroxyl groups, the ferric iron "activates" the substrate by means of abstracting an electron to produce a radical on the substrate. (wikipedia.org)