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表单
powder
储存温度
−20°C
SMILES字符串
CN1c2cc(C)c(C)cc2N=C3C(=O)NC(=O)N=C13
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生化/生理作用
Lumiflavine (Lumiflavin) is produced by the photolysis of vitamin B2 (Riboflavin). Lumiflavine, a riboflavin uptake inhibitor, is used to study riboflavin uptake in intestinal epithelial (Caco-2) and other epithelial cells.
警示用语：
Warning
危险声明
危险分类
Muta. 2
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
N B Sankaran et al.
The journal of physical chemistry. B, 113(5), 1522-1529 (2009-01-30)
The binding behavior of lumiflavin, a biologically vital ligand, with DNA duplexes containing an abasic (AP) site and various target nucleobases opposite the AP site is studied. Lumiflavin binds selectively to thymine (T) opposite the AP site in a DNA
Valeria Bafunno et al.
The Journal of biological chemistry, 279(1), 95-102 (2003-10-14)
We have studied the functional steps by which Saccharomyces cerevisiae mitochondria can synthesize FAD from cytosolic riboflavin (Rf). Riboflavin uptake into mitochondria took place via a mechanism that is consistent with the existence of (at least two) carrier systems. FAD
Hamid M Said et al.
The Journal of physiology, 566(Pt 2), 369-377 (2005-05-10)
In mammalian cells (including those of the ocular system), the water-soluble vitamin B2 (riboflavin, RF) assumes an essential role in a variety of metabolic reactions and is critical for normal cellular functions, growth and development. Cells of the human retinal
Vincent Sichula et al.
The journal of physical chemistry. B, 114(29), 9452-9461 (2010-07-06)
We investigated the oxidation behavior of 5-ethyl-4a-hydroxy-3-methyl-4a,5-dihydrolumiflavin (pseudobase Et-FlOH) in acetonitrile with the aim of determining if the two-electron oxidized Et-FlOH(2+) undergoes a release of hydroxyl cation and the production of 5-ethyl-3methyllumiflavinium cation (Et-Fl(+)). The focus of this work is
Atsuko Satoh et al.
Journal of biochemistry, 134(2), 297-304 (2003-09-11)
The flavoenzyme medium-chain acyl-CoA dehydrogenase (MCAD) eliminates the alpha-proton of the substrate analog, 3-thiaoctanoyl-CoA (3S-C8-CoA), to form a charge-transfer complex with deprotonated 3S-C8-CoA. This complex can simulate the metastable reaction intermediate immediately after the alpha-proton elimination of a substrate and
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