Report

Single-Molecule Enzymatic Dynamics

Science  04 Dec 1998:
Vol. 282, Issue 5395, pp. 1877-1882
DOI: 10.1126/science.282.5395.1877

You are currently viewing the abstract.

View Full Text

Via your Institution

Log in through your institution

Log in through your institution


This article has a correction. Please see:

Abstract

Enzymatic turnovers of single cholesterol oxidase molecules were observed in real time by monitoring the emission from the enzyme's fluorescent active site, flavin adenine dinucleotide (FAD). Statistical analyses of single-molecule trajectories revealed a significant and slow fluctuation in the rate of cholesterol oxidation by FAD. The static disorder and dynamic disorder of reaction rates, which are essentially indistinguishable in ensemble-averaged experiments, were determined separately by the real-time single-molecule approach. A molecular memory phenomenon, in which an enzymatic turnover was not independent of its previous turnovers because of a slow fluctuation of protein conformation, was evidenced by spontaneous spectral fluctuation of FAD.

  • * To whom correspondence should be addressed. E-mail: xsxie{at}pnl.gov

View Full Text

Related Content