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• W2320611719 endingPage "1225" @default.
• W2320611719 startingPage "1218" @default.
• W2320611719 abstract "Adenylate kinase shows a conformational transition (OPEN and CLOSED forms) during substrate binding and product release to mediate the phosphoryl transfer between ADP and ATP/AMP. The protein motional characteristics will be useful to construct switching systems of fluorophore properties caused by the catalytic cycle of the enzyme. This paper demonstrates in situ reversible switching of a fluorophore property driven by the conformational transition of the enzyme. The pyrene-conjugated mutant adenylate kinase is able to switch the monomer/excimer emission property of pyrene on addition of ADP or P1P5-di(adenosine-5′)pentaphosphate (Ap5A, a transition state analog). The observation under the dilute condition (∼0.1 μM) indicates that the emission spectral change was caused by the motion of a protein molecule and not led by protein–protein interactions through π–π stacking of pyrene rings. The switching can be reversibly conducted by using hexokinase-coupling reaction. The fashion of the changes in emission intensities at various ligand concentrations is different between ADP, Mg2+-bound ADP, and Mg2+-bound Ap5A. The emission property switching is repeatable by a sequential addition of a substrate in a one-pot process. It is proposed that the property of a synthetic molecule on the enzyme surface is switchable in response to the catalytic cycle of adenylate kinase." @default.
• W2320611719 created "2016-06-24" @default.
• W2320611719 creator A5014980134 @default.
• W2320611719 creator A5051492016 @default.
• W2320611719 creator A5061194371 @default.
• W2320611719 date "2013-06-11" @default.
• W2320611719 modified "2023-10-18" @default.
• W2320611719 title "Reversible Switching of Fluorophore Property Based on Intrinsic Conformational Transition of Adenylate Kinase during Its Catalytic Cycle" @default.
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• W2320611719 doi "https://doi.org/10.1021/bc400160m" @default.
• W2320611719 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23718926" @default.
• W2320611719 hasPublicationYear "2013" @default.
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