Proton transfer at carbon

The viability of living systems requires that C-H bonds of biological molec ules be stable in water, but that there also be a mechanism for shortening the timescale for their heterolytic cleavage through enzymatic catalysis of a variety of catabolic and metabolic reactions. An understanding of the me chanism of enzymatic catalysis of proton transfer at carbon requires the in tegration of results of studies to determine the structure of the enzyme-su bstrate complex with model studies on the mechanism for the non-enzymatic r eaction in water, and the effect of the local protein environment on the st ability of the transition state for this reaction. A common theme is the im portance of electrostatic interactions in providing stabilization of bound carbanion intermediates of enzyme-catalyzed proton-transfer reactions.