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  2. Nicotinamide adenine dinucleotide phosphate - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_adenine_di...

    Some anaerobic organisms use NADP +-linked hydrogenase, ripping a hydride from hydrogen gas to produce a proton and NADPH. [3] Like NADH, NADPH is fluorescent. NADPH in aqueous solution excited at the nicotinamide absorbance of ~335 nm (near UV) has a fluorescence emission which peaks at 445-460 nm (violet to blue).

  3. Nicotinamide adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_adenine_di...

    NAD + and NADH also differ in their fluorescence. Freely diffusing NADH in aqueous solution, when excited at the nicotinamide absorbance of ~335 nm (near-UV), fluoresces at 445–460 nm (violet to blue) with a fluorescence lifetime of 0.4 nanoseconds, while NAD + does not fluoresce.

  4. Monodehydroascorbate reductase (NADH) - Wikipedia

    en.wikipedia.org/wiki/Monodehydroascorbate...

    The 3 substrates of this enzyme are NADH, H +, and monodehydroascorbate, whereas its two products are NAD + and ascorbate. This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH, with a quinone or similar compound as an acceptor. The systematic name of this enzyme class is NADH: monodehydroascorbate ...

  5. Autofluorescence - Wikipedia

    en.wikipedia.org/wiki/Autofluorescence

    Micrograph of paper autofluorescing under ultraviolet illumination. The individual fibres in this sample are around 10 μm in diameter.. Autofluorescence is the natural emission of light by biological structures such as mitochondria and lysosomes when they have absorbed light, and is used to distinguish the light originating from artificially added fluorescent markers (fluorophores).

  6. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    An example of these assays is again the use of the nucleotide coenzymes NADH and NADPH. Here, the reduced forms are fluorescent and the oxidised forms non-fluorescent. Oxidation reactions can therefore be followed by a decrease in fluorescence and reduction reactions by an increase. [ 5 ]

  7. NADH kinase - Wikipedia

    en.wikipedia.org/wiki/NADH_kinase

    Thus, the two substrates of this enzyme are ATP and NADH, whereas its two products are ADP and NADPH. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:NADH 2'-phosphotransferase.

  8. FMN reductase (NADH) - Wikipedia

    en.wikipedia.org/wiki/FMN_reductase_(NADH)

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  9. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    For instance, native fluorescence of a FAD and NADH is varied in normal tissue and oral submucous fibrosis, which is an early sign of invasive oral cancer. [31] Doctors therefore have been employing fluorescence to assist in diagnosis and monitor treatment as opposed to the standard biopsy .