On the rates of enzymatic, protein and model compound reactions: the importance of diffusion control.
A meaningful method of comparison is suggested for saturation kinetics, typical of enzyme-catalyzed reactions, and nonsaturation kinetics, often typical of model compound reactions. True diffusion-controlled reactions do not give saturation behavior; but enzymes may need saturation behavior to attain selectivity and stereospecificity for complicated substrates or for reactions beyond the complexity of electron transfer. However, the diffusion controlled limit provides a better reference point for rate comparisons than does the rate of uncatalyzed reaction. The failure of the Stokes-Einstein equation for small substrates is documented, as are ways of circumventing the problem. Advantages and pitfalls in the use of viscosogens to test for diffusion control are delineated. Finally, the possible advantages of surface diffusion for an enzyme, but lack of experimental evidence, is discussed.
D004058:Diffusion; D003576:Electron Transport Complex IV / Q000378:metabolism; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D011506:Proteins / Q000378:metabolism*; D012997:Solvents
D004798:Enzymes; D011506:Proteins; D012997:Solvents; D003576:Electron Transport Complex IV