Enzyme catalysis hydrogen formation

First assumptions as to the possibility of hydrogen changing its position in the process of transformation of one chemical particle into another one were voiced nearly 200 years ago [31], and the mechanism of this enormously important reaction has been attracting attention ever since. The reason for this interest is obvious seeing that the proton transfer reactions underlie the acid-base equilibria and determine the mechanisms of a broad range of biological phenomena such as the transport across membranes, enzymic catalysis, photosynthesis, the formation of the ATP acid, spontaneous mutations etc. 

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-... 

The analysis (Fersht, 1988) of hydrogen-bond strengths and of the magnitude of their effect on catalysis can be illustrated with reference to the simplified scheme in (51)-(53). The first step is the formation of an enzyme-... 

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