Proton transfer at carbon.
The viability of living systems requires that C--H bonds of biological molecules 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 mechanism of enzymatic catalysis of proton transfer at carbon requires the integration of results of studies to determine the structure of the enzyme-substrate complex with model studies on the mechanism for the non-enzymatic reaction in water, and the effect of the local protein environment on the stability of the transition state for this reaction. A common theme is the importance of electrostatic interactions in providing stabilization of bound carbanion intermediates of enzyme-catalyzed proton-transfer reactions.
Richard
J P
JP
Department of Chemistry, University at Buffalo, SUNY, Buffalo, NY 14260-3000, USA. jrichard@chem.buffalo.edu
Amyes
T L
TL
D000596:Amino Acids / Q000737:chemistry; D002244:Carbon / Q000737:chemistry*; D002264:Carboxylic Acids / Q000737:chemistry; D002384:Catalysis; D004798:Enzymes / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D010751:Phosphopyruvate Hydratase / Q000737:chemistry; D011522:Protons; D013438:Sulfhydryl Compounds / Q000737:chemistry
D000596:Amino Acids; D002264:Carboxylic Acids; D004798:Enzymes; D011522:Protons; D013438:Sulfhydryl Compounds; D002244:Carbon; D010751:Phosphopyruvate Hydratase