Time-resolved fluorescence experiments have shown that flavin adenine dinucleotide (FAD) fluorescence emission of sol-gel immobilized glucose oxidase (GOD) exhibits a three-exponential decaying behaviour characterized by long- (about 2.0-3.0 ns), intermediate- (about 300 ps) and short- (less than 10 ps) lifetime, each one being characteristic of a peculiar conformational state of the FAD structure. In the present work time-resolved fluorescence is used to monitor FAD signals in the time interval immediately following the addition of glucose at various concentrations in order to detect the conformational changes occurring during the interaction between sol-gel immobilized GOD and glucose. The analysis of time-dependent fluorescence emission signal has shown that the FAD conformational state changes during the process from a configuration with a prevalence of the state characterized by the long lifetime to a configuration with increased contribution from the process with the intermediate lifetime. The time needed to complete this configuration change decreases with the concentration of added glucose. The results here reported indicate that time-resoled fluorescence can be extremely useful for a better understanding of solid phase biocatalysis that is particularly important in light of their clinical and biotechnological applications.
Significance: Cellular metabolic dynamics can occur within milliseconds, yet there are no optimal tools to spatially and temporally capture these events. Autofluorescence imaging can provide metabolic information on the cellular level due to the intrinsic fluorescence of reduced nicotinamide adenine dinucleotide (phosphate) [NAD(P)H] and flavin adenine dinucleotide (FAD).
Aim: Our goal is to build and evaluate a widefield microscope optimized for rapid autofluorescence imaging of metabolic changes in cells.
Recent studies and suggest that flavin adenine dinucleotide (FAD) on its own might be able to act as a biological magnetic field sensor. Motivated by these observations, in this study, we develop a detailed quantum theoretical model for the radical pair mechanism (RPM) for the flavin adenine biradical within the FAD molecule. We use the results of existing molecular dynamics simulations to determine the time-varying distance between the radicals on FAD, which we then feed into a quantum master equation treatment of the RPM.
Purpose: Drug photodegradation is a matter of great concern because it can result in potency loss and adverse side effects. This study examines the light-induced degradation of dacarbazine catalyzed by vitamin B and flavin adenine dinucleotide (FAD) under light-emitting diode (LED) or fluorescent light irradiation.
Methods: Dacarbazine was irradiated with LED (405 nm) or fluorescent light in the presence of various equivalents of vitamin B or FAD.
Iron-based materials have demonstrated significant efficacy in catalyzing hydrogen peroxide (HO) for the removal of antibiotics from aquatic environments. Green rust (GR), a hybrid valence state iron-based catalyst, was synthesized. By exploiting the catalytic properties of glucose oxidase (GOx) to generate HO from glucose (Glu), a GR-GOx/Glu system for the removal of recalcitrant organic compound 4-chlorophenol (4-CP) was constructed.
IFIT proteins (interferon-induced proteins with tetratricopeptide repeats) are key components of the innate immune response that bind to viral and cellular RNA targets to inhibit viral translation and replication. The RNA target recognition is guided by molecular patterns, particularly at the RNA 5' ends. IFIT1 preferably binds RNAs modified with the 7-methylguanosine (m7G) cap-0 structure, while RNAs with cap-1 structure are recognized with lower affinity.
