PerspectiveChemistry

The Motions of an Enzyme Soloist

Science  10 Oct 2003:
Vol. 302, Issue 5643, pp. 239-240
DOI: 10.1126/science.1090850

You are currently viewing the summary.

View Full Text

Via your Institution

Log in through your institution

Log in through your institution


Summary

Dynamics of proteins are crucial to their function. In his Perspective, Orrit stresses the advantages of studying these dynamics with single-molecule methods--which require no synchronization--rather than with conventional ensemble measurements. He highlights the report by Yang et al., who follow the fluorescence of a single enzyme molecule. Electron transfer from the fluorophore to a quencher induces fluctuations of the fluorescence lifetime along with the fluorophore-quencher distance. The wide range of characteristic times of those fluctuations reveals the complexity of the protein's potential energy landscape. As a new molecular ruler, electron transfer complements other single-molecule methods such as energy transfer (FRET) for distances shorter than a few nanometers.

Related Content