Search results
Results from the WOW.Com Content Network
[12] [13] These changes in fluorescence are also used to measure changes in the redox state of living cells, through fluorescence microscopy. [14] NADH can be converted to NAD+ in a reaction catalysed by copper, which requires hydrogen peroxide. Thus, the supply of NAD+ in cells requires mitochondrial copper(II). [15] [16]
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).
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).
A simplified Jablonski diagram illustrating the change of energy levels.. The principle behind fluorescence is that the fluorescent moiety contains electrons which can absorb a photon and briefly enter an excited state before either dispersing the energy non-radiatively or emitting it as a photon, but with a lower energy, i.e., at a longer wavelength (wavelength and energy are inversely ...
This enzyme belongs to the family of oxidoreductases, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. The systematic name of this enzyme is NADPH:NAD+ oxidoreductase (Si-specific). Other names in common use include non-energy-linked transhydrogenase, NAD(P)+ transhydrogenase (B-specific), and soluble transhydrogenase.
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 ...
[1] [2] "Fluorescence microscope" refers to any microscope that uses fluorescence to generate an image, whether it is a simple set up like an epifluorescence microscope or a more complicated design such as a confocal microscope, which uses optical sectioning to get better resolution of the fluorescence image.
Ferredoxin: NADP + reductase is the last enzyme in the transfer of electrons during photosynthesis from photosystem I to NADPH. [2] The NADPH is then used as a reducing equivalent in the reactions of the Calvin cycle. [2] Electron cycling from ferredoxin to NADPH only occurs in the light in part because FNR activity is inhibited in the dark. [11]