Fluorescence quenching studies of structure and dynamics in calmodulin-eNOS complexes
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Issue Date
2015-05-08Article Version
Scholarly/refereed, author accepted manuscript
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Activation of endothelial nitric oxide synthase (eNOS) by calmodulin (CaM) facilitates formation of a sequence of conformational states that is not well understood. Fluorescence decays of fluorescently labeled CaM bound to eNOS reveal four distinct conformational states and single-molecule fluorescence trajectories show multiple fluorescence states with transitions between states occurring on time scales of milliseconds to seconds. A model is proposed relating fluorescence quenching states to enzyme conformations. Specifically, we propose that the most highly quenched state corresponds to CaM docked to an oxygenase domain of the enzyme. In single-molecule trajectories, this state occurs with time lags consistent with the oxygenase activity of the enzyme.
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This is the peer reviewed version of the following article: Arnett David C.,Persechini Anthony,Tran Quang-Kim,Black D.J. and Johnson Carey K.(2015), Fluorescence quenching studies of structure and dynamics in calmodulin–eNOS complexes, FEBS Letters, 589, doi: 10.1016/j.febslet.2015.03.035, which has been published in final form at http://doi.org/10.1016/j.febslet.2015.03.035. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
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Arnett David C.,Persechini Anthony,Tran Quang-Kim,Black D.J. and Johnson Carey K.(2015), Fluorescence quenching studies of structure and dynamics in calmodulin–eNOS complexes, FEBS Letters, 589, doi: 10.1016/j.febslet.2015.03.035
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