Ethyl hydroperoxide, decomposition catalase

Ethyl disulfide, IV, 95 Ethyl hydroperoxide, decomposition by catalase, V, 53... 

Concerning the mode of formation of ES, we prefer the concept that the substrate in a monolayer is chemisorbed to the active center of the enzyme protein, just as the experimental evidence pertaining to surface catalysis by inorganic catalysts indicates that in these reactions chemisorbed, not physically adsorbed, reactants are involved. Such a concept is supported by the demonstration of spectroscopically defined unstable intermediate compounds between enzyme and substrate in the decomposition by catalase of ethyl hydroperoxide,11 and in the interaction between peroxidase and hydrogen peroxide.18 Recently Chance18 determined by direct photoelectric measurements the dissociation con-... 

A property all the primary complexes have in common is the decomposition giving free catalase which does follow first order kinetics (Chance, 71). The velocity constants for ethyl and methyl hydroperoxides are 0.04 and 0.016 sec.-1 as compared with 0.02 sec.-1 for the hydrogen peroxide complex. The secondary complexes decompose far more slowly, the first order velocity constants for ethyl and methyl hydroperoxides having the values 2.3 X 10-4 and 4 X 10-6 sec.-1, respectively. 

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See also in sourсe #XX -- [ ]

See also in sourсe #XX -- [ ]

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