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Biological oxidation, hydrocarbons cytochrome

Biologically, hydrocarbons are oxidized to alcohols or epoxides by molecular oxygen in the presence of cytochromes P-450, which contain Fe(PPIX) as a prosthetic group coordinated by a cysteinyl mercaptide (Scheme 29). [Pg.844]

Biological systems overcome the inherent unreactive character of 02 by means of metalloproteins (enzymes) that activate dioxygen for selective reaction with organic substrates. For example, the cytochrome P-450 proteins (thiolated protoporphyrin IX catalytic centers) facihtate the epoxidation of alkenes, the demethylation of Al-methylamines (via formation of formaldehyde), the oxidative cleavage of a-diols to aldehydes and ketones, and the monooxygenation of aliphatic and aromatic hydrocarbons (RH) (equation 104). The methane monooxygenase proteins (MMO, dinuclear nonheme iron centers) catalyze similar oxygenation of saturated hydrocarbons (equation 105). ... [Pg.3476]

See other pages where Biological oxidation, hydrocarbons cytochrome is mentioned: [Pg.265]    [Pg.441]    [Pg.18]    [Pg.183]    [Pg.169]    [Pg.383]    [Pg.98]    [Pg.367]    [Pg.256]    [Pg.54]    [Pg.299]    [Pg.26]    [Pg.75]    [Pg.449]    [Pg.304]    [Pg.316]    [Pg.444]    [Pg.316]    [Pg.126]    [Pg.268]    [Pg.296]    [Pg.105]   
See also in sourсe #XX -- [ Pg.265 , Pg.266 , Pg.267 , Pg.268 , Pg.269 ]



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