Protein Conformational Dynamics Probed by Single-Molecule Electron Transfer

Electron transfer is used as a probe for angstrom-scale structural changes in single protein molecules. In a flavin reductase, the fluorescence of flavin is quenched by a nearby tyrosine residue by means of photo-induced electron transfer. By probing the fluorescence lifetime of the single flavin on...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2003-10, Vol.302 (5643), p.262-266
Main Authors: Yang, Haw, Luo, Guobin, Karnchanaphanurach, Pallop, Louie, Tai-Man, Rech, Ivan, Cova, Sergio, Xun, Luying, Xie, X. Sunney
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Azines
Biochemistry
Biological and medical sciences
Catalysis
Catalysts
Chemical Phenomena
Chemical reactions
Chemistry, Physical
Computer Simulation
Conformational dynamics in molecular biology
Correlation
Electric properties
Electron transfer
Electrons
Enzymes
Escherichia coli - enzymology
Flavin Mononucleotide - chemistry
Flavin Mononucleotide - metabolism
Flavin-Adenine Dinucleotide - chemistry
Flavin-Adenine Dinucleotide - metabolism
Flavins
Fluorescence
FMN Reductase - chemistry
FMN Reductase - genetics
FMN Reductase - metabolism
Fundamental and applied biological sciences. Psychology
Histograms
Hydrogen Bonding
Likelihood Functions
Mathematics
Models, Molecular
Molecular biophysics
Molecular Structure
Molecules
Mutagenesis, Site-Directed
Photons
Protein Conformation
Proteins
Rapid quenching
Serine
Spectrometry, Fluorescence
Temperature
Thermodynamics
Tyrosine
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Summary:Electron transfer is used as a probe for angstrom-scale structural changes in single protein molecules. In a flavin reductase, the fluorescence of flavin is quenched by a nearby tyrosine residue by means of photo-induced electron transfer. By probing the fluorescence lifetime of the single flavin on a photon-by-photon basis, we were able to observe the variation of flavin-tyrosine distance over time. We could then determine the potential of mean force between the flavin and the tyrosine, and a correlation analysis revealed conformational fluctuation at multiple time scales spanning from hundreds of microseconds to seconds. This phenomenon suggests the existence of multiple interconverting conformers related to the fluctuating catalytic reactivity.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1086911