title: Chemistry. The motions of an enzyme soloist.
abstract: 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.
authors.affiliation: NanoOptics and Spins, Leiden Institute of Physics, Leiden University, Post Office Box 9504, Netherlands. orrit@molphys.leidenuniv.nl
authors.forename: Michel
authors.initials: M
authors.lastname: Orrit
mesh_terms: D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004583:Electrons; D004926:Escherichia coli / Q000201:enzymology; D038181:FMN Reductase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005486:Flavin Mononucleotide / Q000737:chemistry* / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry* / Q000378:metabolism; D005415:Flavins / Q000737:chemistry; D005453:Fluorescence; D006860:Hydrogen Bonding; D007834:Lasers; D016013:Likelihood Functions; D008433:Mathematics; D009154:Mutation; D017785:Photons; D011487:Protein Conformation; D012694:Serine / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013816:Thermodynamics; D014443:Tyrosine
chemical_list: D005415:Flavins; D005182:Flavin-Adenine Dinucleotide; D014443:Tyrosine; D012694:Serine; C008173:isoalloxazine; D005486:Flavin Mononucleotide; D038181:FMN Reductase