Vancraenenbroeck, ReneĢe Webb, Martin R. A Fluorescent, Reagentless Biosensor for ATP, Based on Malonyl-Coenzyme A Synthetase A fluorescent reagentless biosensor for ATP has been developed, based on malonyl-coenzyme A synthetase from <i>Rhodopseudomonas palustris</i> as the protein scaffold and recognition element. Two 5-iodoacetamidotetramethylrhodamines were covalently bound to this protein to provide the readout. This adduct couples ATP binding to a 3.7-fold increase in fluorescence intensity with excitation at 553 nm and emission at 575 nm. It measures ATP concentrations with micromolar sensitivity and is highly selective for ATP relative to ADP. Its ability to monitor enzymatic ATP production or depletion was demonstrated in steady-state kinetic assays in which ATP is a product or substrate, respectively. Reagentless Biosensor;ATP production;575 nm;protein scaffold;micromolar sensitivity;reagentless biosensor;adduct couples ATP binding;553 nm;measures ATP concentrations;fluorescence intensity;Rhodopseudomonas palustris;ADP;recognition element 2015-12-17
    https://acs.figshare.com/articles/journal_contribution/A_Fluorescent_Reagentless_Biosensor_for_ATP_Based_on_Malonyl_Coenzyme_A_Synthetase/2006025
10.1021/acschembio.5b00346.s001