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Science 10 October 2003:
Vol. 302. no. 5643, pp. 239 - 240
DOI: 10.1126/science.1090850
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Perspectives

CHEMISTRY:
The Motions of an Enzyme Soloist

Michel Orrit

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.

The author is with Molecular NanoOptics and Spins, Leiden Institute of Physics, Leiden University, Post Office Box 9504, Netherlands. E-mail: orrit{at}molphys.leidenuniv.nl

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Science. ISSN 0036-8075 (print), 1095-9203 (online)