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Heme monooxygenase

Most characteristic for the catalytic cycle of heme monooxygenases is the activation of molecular dioxygen to an active FeO moiety and water. Only two out of four oxidation equivalents are thus used for the synthesis of oxygenated products. This fact is often used as a mechanistic possibility of a short-cut, the so-called peroxide shunt, where a... [Pg.49]

Fig. 6.46 Dendritic Fem porphyrins as model compounds for heme monooxygenases (according to Diederich et at.)... Fig. 6.46 Dendritic Fem porphyrins as model compounds for heme monooxygenases (according to Diederich et at.)...
A. G. Katopodis, K. Wimalasena, J. Lee, and S. W. May, Mechanistic studies on non-heme monooxygenase catalysis Epoxidation, aldehyde formation, and demethylation by the omega-hydroxylation system of Pseudomonas oleo-vorans, J. Am. Chem. Soc., 206 7928 (1984). [Pg.238]

Shimada, H., S.G. Sligar, H. Yeom, H. and Y. Ishimura (1997). Heme monooxygenases. A chemical mechanism for cytochrome P450 oxygen activation. Catalysis by Metal Complexes, 19, 195-221. [Pg.174]

Many other recent works have been devoted to the mechanisms of oxidations catalyzed by non-heme monooxygenases [33], See also a special issue of Journal of Biological Inorganic Chemistry (JBIC) containing papers on the mechanism of methane monooxygenase [30d, 34],... [Pg.481]

Davydov R, Hoffman BM (2011) Active intermediates in heme monooxygenase reactions as revealed by cryoieduction/annealing, EPR/ENDOR studies. Arch Biochem Biophys 507 36—43... [Pg.104]

Grinkova YV, Denisov IG, McLean MA, Sligar SG (2013) Oxidase uncoupling in heme monooxygenases human cytochrome P450 CYP3A4 in nanodiscs. Biochem Biophys Res Commun 430 1223-1227... [Pg.110]

Xu F, Bell SG, Lednik J, Insley A, Rao Z, Wong LL (2005) The heme monooxygenase cytochrome P450cam can be engineered to oxidize ethane to ethanol. Angew Chem Int Ed Engl 44 4029-4032... [Pg.508]


See other pages where Heme monooxygenase is mentioned: [Pg.95]    [Pg.416]    [Pg.50]    [Pg.239]    [Pg.518]    [Pg.519]    [Pg.519]    [Pg.145]    [Pg.1908]    [Pg.151]    [Pg.161]    [Pg.162]    [Pg.163]    [Pg.758]    [Pg.161]    [Pg.162]    [Pg.163]    [Pg.164]    [Pg.149]    [Pg.156]    [Pg.1907]    [Pg.483]    [Pg.495]    [Pg.406]    [Pg.7]    [Pg.195]    [Pg.197]    [Pg.199]    [Pg.201]    [Pg.203]    [Pg.205]    [Pg.207]    [Pg.209]    [Pg.211]    [Pg.213]    [Pg.215]    [Pg.217]    [Pg.219]    [Pg.222]    [Pg.223]    [Pg.227]   
See also in sourсe #XX -- [ Pg.240 ]

See also in sourсe #XX -- [ Pg.7 , Pg.223 ]




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Heme groups monooxygenase

Heme groups monooxygenases

Heme type monooxygenases

Heme-dependent monooxygenases

Heme-thiolate monooxygenase

Monooxygenase heme containing

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