Fluorescence quenching studies of structure and dynamics in calmodulin-eNOS complexes

Arnett, David C.; Persechini, Anthony; Tran, Quang-Kim; Black, D. J.; Johnson, Carey K.

dc.contributor.author	Arnett, David C.
dc.contributor.author	Persechini, Anthony
dc.contributor.author	Tran, Quang-Kim
dc.contributor.author	Black, D. J.
dc.contributor.author	Johnson, Carey K.
dc.date.accessioned	2017-06-12T20:13:57Z
dc.date.available	2017-06-12T20:13:57Z
dc.date.issued	2015-05-08
dc.identifier.citation	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	en_US
dc.identifier.uri	http://hdl.handle.net/1808/24477
dc.description	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.	en_US
dc.description.abstract	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.	en_US
dc.publisher	Wiley	en_US
dc.title	Fluorescence quenching studies of structure and dynamics in calmodulin-eNOS complexes	en_US
dc.type	Article	en_US
kusw.kuauthor	Arnett, David C.
kusw.kuauthor	Johnson, Carey K.
kusw.kudepartment	Chemistry	en_US
dc.identifier.doi	10.1016/j.febslet.2015.03.035	en_US
kusw.oaversion	Scholarly/refereed, author accepted manuscript	en_US
kusw.oapolicy	This item meets KU Open Access policy criteria.	en_US
dc.identifier.pmid	PMC4426000	en_US
dc.rights.accessrights	openAccess

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