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质量水平
方案
96%
表单
powder
SMILES字符串
O=C1NC(=O)c2nc3ccccc3nc2N1
InChI
1S/C10H6N4O2/c15-9-7-8(13-10(16)14-9)12-6-4-2-1-3-5(6)11-7/h1-4H,(H2,12,13,14,15,16)
InChI key
HAUGRYOERYOXHX-UHFFFAOYSA-N
基因信息
human ... ADORA1(134) , ADORA2A(135) , ADORA2B(136)
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储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
从最新的版本中选择一种：
分析证书(COA)
Lot/Batch Number
Hideaki Takahashi et al.
The Journal of chemical physics, 129(20), 205103-205103 (2008-12-03)
The isoalloxazine ring (flavin ring) is a part of the coenzyme flavin adenine dinucleotide and acts as an active site in the oxidation of a substrate. We have computed the free energy change Deltamicro(red) associated with one-electron reduction of the
Su Ma et al.
Microbial cell factories, 16(1), 37-37 (2017-03-02)
Cellobiose dehydrogenase (CDH) is an extracellular enzyme produced by lignocellulolytic fungi. cdh gene expression is high in cellulose containing media, but relatively low CDH concentrations are found in the supernatant of fungal cultures due to strong binding to cellulose. Therefore
Shuxia Chen et al.
PloS one, 8(11), e79730-e79730 (2013-11-16)
Two phenolic compound parameters (total phenolic and flavonoid contents) and 5 antioxidant parameters (DPPH [2, 2-diphenyl-1-picrylhydrazyl] radical scavenging activity, HRSC (hydroxyl radical scavenging capacity), FRAP (ferric ion reducing antioxidant power), CUPRAC (cupric ion reducing antioxidant capacity), and MCA (metal chelating
Olayinka O Ogunro et al.
Nano letters, 9(3), 1034-1038 (2009-02-25)
We have studied the structural and electronic stability of a helical ribbon of flavin mononucleotide wrapping around single-walled carbon nanotubes using first-principles density-functional calculations. The helical ribbon is formed through hydrogen bonding between adjacent uracil moieties of the isoalloxazine ring
Stefan Weber et al.
Photochemistry and photobiology, 87(3), 574-583 (2011-01-05)
Blue-light sensitive photoreceptory BLUF domains are flavoproteins, which regulate various, mostly stress-related processes in bacteria and eukaryotes. The photoreactivity of the flavin adenine dinucleotide (FAD) cofactor in three BLUF domains from Rhodobacter sphaeroides, Synechocystis sp. PCC 6803 and Escherichia coli
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