Solar energy is the most abundant and clean on earth, developing equipment or devices with high-efficiency solar conversion an effective way to alleviate crisis. The majority of redox enzymes require a coenzyme provide hydrogen source needed for reaction process, commonly used nicotinamide adenine dinucleotide (NADH). However, NADH expensive easily decomposed, which greatly limits its applicati...

We describe some characteristics of the mode of formation of inhibitors of lactate dehydrogenase from commercial NADH. Inhibitor formation is time- and concentration-dependent and also varies with the commercial source of NADH. At least two inhibitory components can form in concentrated NADH solutions. One of these can be separated from NADH by chromatography on either diethylaminoethyl-celluos...

Oxygen supply implies higher production cost and reduction of maximum theoretical yields. Thus, generation fermentation products is more cost-effective. Aiming to find a key piece for the (poly)-3-hydroxybutyrate (PHB) as product, here we characterize an acetoacetyl-CoA reductase, isolated from Candidatus Accumulibacter phosphatis-enriched mixed culture, showing (kcatNADH/KMNADH)/(kcatNADPH/KMN...

Ischaemia decreases mitochondrial NADH oxidation, activates glycolysis, increases the NADH/NAD+ ratio, and causes lactate production. The mechanisms that regulate anaerobic glycolysis and the NADH/NAD+ ratio during ischaemia are unclear. Although continuous measurements of metabolic fluxes and NADH/NAD+ in cytosol and mitochondria are not possible in vivo with current experimental techniques, c...

The low yield of enzymatic conversion CO2 to formic acid as well the high cost and instability using natural cofactor (NADH) hamper large-scale application utilization. To address these issues improve production acid, six bipyridinium-based artificial cofactors were developed for further integrated with electrocatalytic regeneration production. All them did show a higher catalytic performance c...

Biochemical estimation of NADH concentration is a useful method for monitoring cellular metabolism, because the NADH/NAD+ reduction-oxidation pair is crucial for electron transfer in the mitochondrial electron chain. In this article, we present a novel method for deriving functional maps of intracellular reduction-oxidation ratio in vivo via measurement of the fluorescence lifetimes and the rat...

Reduction of NAD+ by dehydrogenase enzymes to form NADH is a key component of cellular metabolism. In cellular preparations and isolated mitochondria suspensions, enzyme-dependent fluorescence recovery after photobleaching (ED-FRAP) of NADH has been shown to be an effective approach for measuring the rate of NADH production to assess dehydrogenase enzyme activity. Our objective was to demonstra...

NADH oxidase-overproducing Lactococcus lactis strains were constructed by cloning the Streptococcus mutans nox-2 gene, which encodes the H2O-forming NADH oxidase, on the plasmid vector pNZ8020 under the control of the L. lactis nisA promoter. This engineered system allowed a nisin-controlled 150-fold overproduction of NADH oxidase at pH 7.0, resulting in decreased NADH/NAD ratios under aerobic ...

Cytosolic free NAD/NADH ratio is fundamentally important in maintaining cellular redox homeostasis but current techniques cannot distinguish between protein-bound and free NAD/NADH. Williamson et al reported a method to estimate this ratio by cytosolic lactate/pyruvate (L/P) based on the principle of chemical equilibrium. Numerous studies used L/P ratio to estimate the cytosolic free NAD/NADH r...

We investigated whether and how mitochondria from durum wheat (Triticum durum Desf.) and potato (Solanum tuberosum), isolated from etiolated shoots and a cell suspension culture, respectively, oxidize externally added NADH via the mitochondrial shuttles; in particular, we compared the shuttles and the external NADH dehydrogenase (NADH DHExt) with respect to their capacity to oxidize external NA...