Quantitative interpretation of the randomness in single enzyme turnover times.

Fluctuating turnover times of a single enzyme become observable with the advent of modern cutting-edge, single enzyme experimental techniques. Although the conventional chemical kinetics and its modern generalizations could provide a good quantitative description for the mean of the enzymatic turnover times, to our knowledge there has not yet been a successful quantitative interpretation for the variance or the randomness of the enzymatic turnover times. In this review, we briefly review several theories in this field, and compare predictions of these theories to the randomness parameter data reported for β-galactosidase enzyme. We find the recently proposed kinetics for renewal reaction processes could provide an excellent quantitative interpretation of the randomness parameter data. From the analysis of the randomness parameter data of the single enzyme reaction, one can extract quantitative information about the mean lifetime of enzyme-substrate complex; the success or the failure probability of the catalytic reaction per each formation of ES complex; and the non-Poisson character of the reaction dynamics of the ES complex (which is beyond reach of the long-standing paradigm of the conventional chemical kinetics).