In biochemistry, flavin adenine dinucleotide (FAD) is a redox -active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may …

2008年10月2日 · The tricyclic isoalloxazine nucleus of the redox cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) acts as an electron sink in life-sustaining biological electron transfer...

2024年12月1日 · Recent studies in vitro and in vivo 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.

2019年1月1日 · In detail, the neutral FAD radical of Escherichia coli CPD photolyase (EcPL) (Fuchs et al., 2002) is compared with anionic and neutral flavin radicals of Aspergillus niger glucose oxidase (GO) (Okafuji et al., 2008) and NADH-ubiquinone oxidoreductase (NQR) (Barquera et al., 2003).

2006年7月18日 · We show that formation of the red-shifted signaling state proceeds by means of a radical-pair mechanism, driven by ET and PT processes to FAD from its protein environment and resulting in the transient formation of anionic and neutral FAD radical species.

FAD or flavin adenine dinucleotide is a very common coenzyme (a cofactor made up of organic molecules) in proteins. Similar to NAD and NADP in that it carries electrons, FAD participates in many important chemical reactions that flavoproteins carry out.

2020年7月1日 · Fatty acid photodecarboxylases (FAP) are a recently discovered family of FAD-containing, light-activated enzymes, which convert fatty acids to n-alkanes/alkenes with potential applications in the manufacture of fine and speciality chemicals and fuels. Poor catalytic stability of FAPs is however a major limitation.

We present time-resolved optical absorption and magnetic field effect data on the photochemistry following blue light excitation of flavin adenine dinucleotide (FAD) in aqueous solution in the pH range 2.3 to 8.0.

In this work, we systematically examine the excited-state dynamics of five redox states of flavins from oxidized FAD and FMN, to anionic radical FAD •-, to neutral radical FMNH •, to fully-reduced anionic FADH - and FMNH -, and finally to fully-reduced neutral …

Subsequent long-range, interdomain electron transfer between FAD and flavin mononucleotide (FMN) generates di-radical flavin semiquinone states that form/decay on the (ms–s) timescale. Electron transfer to downstream partner proteins completes the catalytic cycle [35,40].