title: Nonrenewal statistics in the catalytic activity of enzyme molecules at mesoscopic concentrations.
abstract: Recent fluorescence spectroscopy measurements of single-enzyme kinetics have shown that enzymatic turnovers form a renewal stochastic process in which the inverse of the mean waiting time between turnovers follows the Michaelis-Menten equation. We study enzyme kinetics at physiologically relevant mesoscopic concentrations using a master equation. From the exact solution of the master equation we find that the waiting times are neither independent nor identically distributed, implying that enzymatic turnovers form a nonrenewal stochastic process. The inverse of the mean waiting time shows strong departure from the Michaelis-Menten equation. The waiting times between consecutive turnovers are anticorrelated, where short intervals are more likely to be followed by long intervals and vice versa. Correlations persist beyond consecutive turnovers indicating that multiscale fluctuations govern enzyme kinetics.
authors.affiliation: Department of Chemistry, Indian Institute of Technology, Madras, Chennai, India.
authors.forename: Soma
authors.initials: S
authors.lastname: Saha
authors.forename: Somdeb
authors.initials: S
authors.lastname: Ghose
authors.forename: R
authors.initials: R
authors.lastname: Adhikari
authors.forename: Arti
authors.initials: A
authors.lastname: Dua
mesh_terms: D055162:Biocatalysis; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical; D011336:Probability; D013269:Stochastic Processes; D013816:Thermodynamics
chemical_list: D004798:Enzymes