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- W2912487534 abstract "Changes in metabolism in cells are often studied by the ratio of NAD+ to NADH. This ratio is correlated to free and enzyme bound NADH, which can be used as a measurement of metabolic states in cells using fluorescence lifetime imaging (FLIM). Binding of NADH to the enzyme causes separation between nicotinamide and adenine moieties of Nicotinamide adenine dinucleotide (NADH) from their collapsed structure in solution and results in increase of fluorescence quantum yield and lifetime. The extent of increase in fluorescence lifetime is dependent on the apoenzyme and presence of auxiliary ions. Reports from past studies show distinctive discrepancies in calculation of the bound NADH lifetime, often related to complications in sample preparation and limitations in data acquisition. In this work, we show that in presence of oxalic ion, proper preparation of lactate dehydrogenase (LDH) bound NADH has a lifetime of 3.4 ns and is positioned on the universal semi-circle of the phasor plot, representing mono-exponential lifetime. Improper preparation results in a mixture of species, with phasor positions inside the universal semi-circle. Measurement in cellular environment show similar trend and a linear trajectory between free NADH and cellular NADH components, which when extrapolated to the universal semi-circle shows a lifetime of 3.4 ns at the crossing point. These results suggests that 3.4 ns can be used as a bound NADH lifetime and phasor approach can correlate lifetime contributions to concentration fractions of free and bound species. The effects of different types of FLIM acquisitions are also discussed in context. This work is supported by NIH grant P41-GM103540." @default.
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- W2912487534 date "2019-02-01" @default.
- W2912487534 modified "2023-09-25" @default.
- W2912487534 title "The Fluorescence Lifetime of Bound NADH: Clues from the Phasor Plots" @default.
- W2912487534 doi "https://doi.org/10.1016/j.bpj.2018.11.3039" @default.
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