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

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.

SUBMITTER: Arnett DC

PROVIDER: S-EPMC4426000 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

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

Arnett David C DC Persechini Anthony A Tran Quang-Kim QK Black D J DJ Johnson Carey K CK

FEBS letters 20150411 11

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 en ...[more]

PMID: 25871521

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