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Monooxygenases hydrocarbon monooxygenase

Patel RN, CT Hou, AI Laskin, A Felix (1982) Microbial oxidation of hydrocarbons properties of a soluble monooxygenase from a facultative methane-utilizing organisms Methylobacterium sp. strain CRL-26. Appl Environ Microbiol 44 1130-1137. [Pg.86]

Hydrocarbon hydroxylases introducing oxygen into nonoxygenated rings Toluene, phenanthrene, pyrene monooxygenases Hydrocarbon epoxidases... [Pg.104]

Although monooxygenases can be involved in the degradation of toluene, there is a complex relation between toluene monooxygenase activity and the degradation of chlorinated hydrocarbons. [Pg.366]

Oldenhuis R, RLJM Vink, DB Janssen, B Witholt (1989) Degradation of chlorinated aliphatic hydrocarbons by Methylosinus trichosporium OB3b expressing soluble methane monooxygenase. Appl Environ... [Pg.375]

Although the exact mechanism of degradation at metabolic level for each compound or group of compounds is not well known, the involvement of extracellular oxidative enzymes such as LAC, MnP, LiP, and versatile peroxidase (VP) (see Tables 1 and 2 of Chap. 6) and intracellular monooxygenases as cytochrome P-450 is well documented for pollutants such as hydrocarbons, dyes, and halogenated solvents [25]. To determine the actual role of the extracellular enzymes, many studies are performed in vitro experiments with purified enzymes. In the case of cytochrome P-450, usually inhibitors are used. [Pg.283]

Mueller and Miller (33) and Brodie et al. (34) were the first to show that enzymes in the microsomal fraction of rat liver could effectively oxidize xenobiotics. Comparable enzymes (aryl hydrocarbon monooxygenases) were later reported in the hepatic tissues of fresh water and marine fish by Creaven et al. (35) and Buhler and Rasmusson (36). Reconstituted hepatic microsomal systems require cytochrome P-450 for monooxygenase activity in both mammals (37) and fish (38,39). Bend et al. [Pg.64]

Table III. Inhibition of monooxygenase (aryl hydrocarbon hydroxylase) activity in fish and mammalian hepatic microsomes (based on... Table III. Inhibition of monooxygenase (aryl hydrocarbon hydroxylase) activity in fish and mammalian hepatic microsomes (based on...
Transition metal hydroperoxo species are well established as important intermediates in the oxidation of hydrocarbons (8,70,71). As they relate to the active oxygenating reagent in cytochrome P-450 monooxygenase, (porphyrin)M-OOR complexes have come under recent scmtiny because of their importance in the process of (poiphyrin)M=0 formation via 0-0 cleavage processes (72-74). In copper biochemistry, a hydroperoxo copper species has been hypothesized as an important intermediate in the catalytic reaction of the copper monooxygenase, dopamine P-hydroxylase (75,76). A Cu-OOH moiety has also been proposed to be involved in the disproportionation of superoxide mediated by the copper-zinc superoxide dismutase (77-78). Thus, model Cun-OOR complexes may be of... [Pg.96]

Starek A. 1988. [The effect of kerosene hydrocarbons on microsomal monooxygenases activity in rat liver.] Folia Med Cracov 29(3-4) 161-170. (Polish)... [Pg.192]

HYDROGEN TUNNELING HYDROCARBON MONOOXYGENASE HYDROGENASE Hydrogen bonding,... [Pg.749]


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See also in sourсe #XX -- [ Pg.1263 ]




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Aryl hydrocarbon monooxygenases

Hydrocarbon monooxygenase

Hydrocarbon monooxygenase

Methane monooxygenase hydrocarbon hydroxylation

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