cytochrome-c-t has been researched along with methylphenylsulfide* in 1 studies
1 other study(ies) available for cytochrome-c-t and methylphenylsulfide
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New activities of a catalytic antibody with a peroxidase activity: formation of Fe(II)-RNO complexes and stereoselective oxidation of sulfides.
In order to estimate the size of the cavity remaining around the heme of the 3A3-microperoxidase 8 (MP8) hemoabzyme, the formation of 3A3-MP8-Fe(II)-nitrosoalkane complexes upon oxidation of N-monosubstituted hydroxylamines was examined. This constituted a new reaction for hemoabzymes and is the first example of fully characterized Fe(II)-metabolite complexes of antibody-porphyrin. Also, via a comparison of the reactions with N-substituted hydroxylamines of various size and hydrophobicity, antibody 3A3 was confirmed to bring about a partial steric hindrance on the distal face of MP8. Subsequently, the influence of the antibody on the stereoselectivity of the S-oxidation of sulfides was examined. Our results showed that MP8 alone and the antibody-MP8 complex catalyze the oxidation of thioanisole by H(2)O(2) and tert-butyl hydroperoxide, following a peroxidase-like two-step oxygen-transfer mechanism involving a radical-cation intermediate. The best system, associating H(2)O(2) as oxidant and 3A3-MP8 as a catalyst, in the presence of 5% tert-butyl alcohol, led to the stereoselective S-oxidation of thioanisole with a 45% enantiomeric excess in favour of the R isomer. This constitutes the highest enantiomeric excess reported to date for the oxidation of sulfides catalyzed by hemoabzymes. Topics: Animals; Binding Sites; Cytochromes c; Heme; Horses; Hydrogen Peroxide; Hydroxylamines; Iron; Kinetics; Models, Biological; Models, Chemical; Oxygen; Peroxidases; Porphyrins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Stereoisomerism; Sulfides; tert-Butylhydroperoxide; Time Factors; Ultraviolet Rays | 2004 |