1088-56-8

Usage

Uses

Used in Pharmaceutical Industry:
LUMIFLAVINE is used as a research compound for studying the effects and mechanisms of vitamin B2 photolysis, contributing to the development of safer and more effective pharmaceutical formulations.
Used in Chemical Research:
LUMIFLAVINE serves as a valuable chemical intermediate in the synthesis of various compounds and the investigation of photochemical reactions, furthering our understanding of chemical processes and potential applications.

Purification Methods

Lumiflavin forms orange crystals upon recrystallisation from 12% aqueous AcOH, or from formic acid. It sublimes at high vacuum. It is freely soluble in CHCl3, but not very soluble in H2O and most organic solvents. In H2O and CHCl3 solution it has a green fluorescence. UV has max at 269, 355 and 445nm ( 38,800, 11,700 and 11,800, respectively) in 0.1N NaOH and 264, 373 and 440nm ( 34,700, 11,400 and 10,400, respectively) in 0.1N HCl, while the UV in CHCl3 has max at 270, 312, 341, 360, 420, 445 and 470nm. [Hemmerich et al. Helv Chim Acta 39 1242 1956, Holiday & Stern Chem Ber 67 1352 1834, Yoneda et al. Chem Pharm Bull Jpn 20 1832 1972, Birch & Moye J Chem Soc 2622 1958, Fluorescence: Kuhn & Moruzzi Chem Ber 67 888 1934, Beilstein 26 III/IV 2539.]

InChI:InChI=1/C13H12N4O2/c1-6-4-8-9(5-7(6)2)17(3)11-10(14-8)12(18)16-13(19)15-11/h4-5H,1-3H3,(H,16,18,19)

Upstream product

• 61066-33-9 pyrimidine-2,4,5,6(1H,3H)-tetraone 
• 17978-55-1 N¹,4,5-trimethylbenzene-1,2-diamine 
• 699-40-1 5,5-Dichloro-barbituric acid 
• 21079-31-2 carboxylmethylflavin 
• 83-88-5 riboflavin 
• 23542-56-5 N',N''-dihydrolumiflavin 
• 4250-90-2 Formylmethylflavin 
• 7732-18-5 water 
• 146-14-5 flavin adenine dinucleotide 
• 7647-01-0 hydrogenchloride 
• 146-17-8 Flavin mononucleotide 
• 6972-71-0 4,5-dimethyl-2-nitrobenzenamine 
• 17978-54-0 N¹,4,5-trimethyl-2-nitroaniline 
• 3237-50-1 5,5-dihydroxy-pyrimidine-2,4,6-trione 

Downstream Products

• 58017-92-8 5-Acetyl-leukolumiflavin 
• 17978-55-1 N¹,4,5-trimethylbenzene-1,2-diamine 
• 37854-59-4 Ro 08-2750 
• 1452453-29-0 C₁₃H₁₂N₄O₂*C₁₀₉H₁₇₉N₃O₁₀ 
• 67-56-1 methanol 
• 201230-82-2 carbon monoxide 
• 4951-03-5 3-hydroxy-1,6,7-trimethyl-1H-quinoxalin-2-one 
• 159782-01-1 2-methoxy-6,7-dimethyl-quinoxaline-3-carboxylic acid 
• 1214-95-5 1,2-dihydro-2-keto-1,6,7-trimethyl-quinoxaline-3-carboxylic acid 
• 1086-80-2 7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione 
• 57-13-6 urea 
• 84869-39-6 7-carboxylumichrome 
• 340259-04-3 2,3,4,5,6-pentafluorophenyl 2-(5,7,8-trimethyl-1,3-dioxo-2,5-dihydro-2,4-diazaphenazin-2-yl)acetate 
• 20227-26-3 (7,8,10-trimethyl-2,4-dioxo-4,10-dihydro-2H-benzo[g]pteridin-3-yl)acetic acid 

Related news

Molecular associations between LUMIFLAVINE (cas 1088-56-8) and some β-carbolines08/13/2019

The molecular associations between a model flavine and three substituted β-carbolines are calculated using a pair potential approach proposed by Fraga. Stacked minima found through a crossed search procedure are analized and some structural and energetic properties related to the saturation of ...detailed

Relevant academic research and scientific papers

Surface-Enhanced Raman Spectroscopy from Flavins Adsorbed on a Silver Electrode: Observation of the Unstable Semiquinone Intermediate

The surface-enhanced Raman scattering (SERS) spectroscopy of protein-free flavin in different redox states was investigated at a silver electrode.Good-quality spectra for oxidized flavin with an excitation frequency within the absorption band (514.5 or 488 nm) and out of the absorption band (yellow-red region) are reported.Fluorescence interference from the flavin is nearly completely quenched by the surface interaction.Reduced flavin did not exhibit a well-defined SERS spectrum, probably because of the break down of the surface complex.The SERS spectrum of the neutral semiquinone radical, as an intermediate of the two single-electron reduction steps, was observed in acidic solution with yellow or red excitation.The utility of SERS as a technique for probing the existence of an unstable intermediate species at the electrode surface is demonstrated.

15N solid-state NMR provides a sensitive probe of oxidized flavin reactive sites

Flavins are central to the reactivity of a wide variety of enzymes and electron transport proteins. There is great interest in understanding the basis for the different reactivities displayed by flavins in different protein contexts. We propose solid-state nuclear magnetic resonance (SS-NMR) as a tool for directly observing reactive positions of the flavin ring and thereby obtaining information on their frontier orbitals. We now report the SS-NMR signals of the redox-active nitrogens N1 and N5, as well as that of N3. The chemical shift tensor of N5 is over 720 ppm wide, in accordance with the predictions of theory and our calculations. The signal of N3 can be distinguished on the basis of coupling to 1H absent for N1 and N5, as well as the shift tensor span of only 170 ppm, consistent with N3's lower aromaticity and lack of a nonbonding lone pair. The isotropic shifts and spans of N5 and N1 reflect two opposite extremes of the chemical shift range for "pyridine-type" N's, consistent with their electrophilic and nucleophilic chemical reactivities, respectively. Upon flavin reduction, N5's chemical shift tensor contracts dramatically to a span of less than 110 ppm, and the isotropic chemical shift changes by approximately 300 ppm. Both are consistent with loss of N5's nonbonding lone pair and decreased aromaticity, and illustrate the responsiveness of the 15N chemical shift principal values to electronic structure. Thus. 15N chemical shift principal values promise to be valuable tools for understanding electronic differences that underlie variations in flavin reactivity, as well as the reactivities of other heterocyclic cofactors.

Photolysis of carboxymethylflavin in aqueous and organic solvent: A kinetic study

This is the first study on the photolysis of carboxymethylflavin (CMF), an intermediate in the photolysis of riboflavin (RF). CMF is photodegraded by removal of side-chain to lumichrome (LC) in acid solution and to LC and lumiflavin (LF) in alkaline solution. It also undergoes alkaline hydrolysis to 1,2-dihydro-1-methyl-2-keto-3-quinoxaline carboxylic acid (KA) and 1,2,3,4-tetrahydro-1-methyl-2,3-dioxoquinoxaline (DQ) by cleavage of isoalloxazine ring. CMF degrades to LC in organic solvents. The formation of LC in acid solution and organic solvents takes place by second-order reaction and those of LC, LF, KA and DQ in alkaline solution by first-order reactions. The values of second-order rate constants for the photolysis of CMF at pH 2.0 to 7.0 are in the range of 1.13 to 2.45 M-1 s-1 and those of first-order rate constants (kobs) at pH 8.0-12.0 from 1.53 to 4.18 × 10-4 s-1 and for the formation of photoproducts from 0.37 to 16.6 × 10-5 s-1. The photolysis of CMF is enhanced, with pH, in the alkaline region since the excited state is sensitive to alkaline hydrolysis. The photolysis and fluorescence quantum yields of CMF in aqueous and organic solvents have been reported. CMF and photoproducts have been assayed spectrofluorimetrically. The mode of CMF photolysis is discussed.

A Remarkable Oxidative Cascade That Replaces the Riboflavin C8 Methyl with an Amino Group during Roseoflavin Biosynthesis

Roseoflavin is a naturally occurring riboflavin analogue with antibiotic properties. It is biosynthesized from riboflavin in a reaction involving replacement of the C8 methyl with a dimethylamino group. Herein we report the identification of a flavin-dependent enzyme that converts flavin mononucleotide (FMN) and glutamate to 8-amino-FMN via the intermediacy of 8-formyl-FMN. A mechanistic proposal for this remarkable transformation is proposed.

Light activated composite tissue adhesives

Disclosed herein are compositions comprising gelatin, collagen, and a chromophore that produces a reactive oxygen species upon exposure to electromagnetic radiation. These compositions have also been found to be strong tissue adhesives that crosslinks the composition and tissue and are effective in closing and sealing wounds, fixation of grafts/implants and anastomoses.

Riboflavin degradation in the presence of quercetin in methanol under continuous UV-B irradiation: The ESI-MS-UHPLC analysis

The presented work deals with continuous UV-B irradiation of riboflavin in MeOH solution, leading to its degradation under anaerobic as well as aerobic conditions (faster in the former case), which is related to riboflavin photosensitizing properties (type I photosensitizer in the first case, and type II in the other one). Addition of quercetin, a well-known antioxidant in the system causes a decrease of the (riboflavin) degradation in both cases. In anaerobic conditions it might be a consequence of quercetin antioxidant scavenging activity, while under aerobic conditions it could be related to singlet oxygen formation. The degradation dynamics - in both systems, in the presence and in the absence of quercetin - is well synchronized with dynamics formation of the two major products, lumiflavin and lumichrome

Effect of ph, buffer, and viscosity on the photolysis of formylmethylflavin: A kinetic study

The kinetics of the photolysis of formylmethylflavin, a major intermediate product in the aerobic and anaerobic photolysis of riboflavin, was studied in the pH range 2.0-11.0. Formylmethylflavin and its photoproducts, lumichrome and lumiflavin, were determined in degraded solutions using a specific multicomponent spectrophotometric method. The photolysis of formylmethylflavin in alkaline medium takes place by first-order kinetics and the rate constants (kobs) at pH 7.5-11.0 range from 0.27×10-4 to 3.88×10-4 and 0.36×10-4 to 5.63×10-4s-1 under aerobic and anaerobic conditions respectively. In acid medium, the photolysis involves a second-order mechanism and the rate constants at pH 2.0-7.0 range from 1.37 to 2.11 and 2.03 to 2.94M-1s-1 under aerobic and anaerobic conditions respectively. The rate-pH profiles for the photolysis reactions indicate the highest rate of formylmethylflavin degradation is at ～pH 4 and above pH 10. In the alkaline region, the increase in rate with pH is due to higher reactivity of the flavin triplet state. The photolysis of formylmethylflavin is catalyzed by phosphate ions and is affected by the solvent viscosity.

Effect of caffeine complexation on the photolysis of riboflavin in aqueous solution: A kinetic study

The effect of caffeine complexation with riboflavin on the kinetics of riboflavin photolysis in the pH range 2.0-10.5 has been studied. The photolysis of riboflavin solutions (5×10-5 M) was carried out in the presence of caffeine (0.5-2.5x10su

Photoirradiation products of flavin derivatives, and the effects of photooxidation on guanine

Photoirradiation in the presence of riboflavin led to guanine oxidation and the formation of imidazolone. Meanwhile, riboflavin itself was degraded by ultraviolet light A (UV-A) and visible light (VIS) radiation, and the end product was lumichrome. VIS radiation in the presence of riboflavin oxidized guanine similarly to UV-A radiation. Although UV-A radiation with lumichrome oxidized guanine, VIS radiation with lumichrome did not. Thus, UV-A radiation with riboflavin can oxidize guanine even if riboflavin is degraded to lumichrome. In contrast, following VIS radiation degradation of riboflavin to lumichrome, VIS radiation with riboflavin is hardly capable of oxidizing guanine. The consequences of riboflavin degradation and guanine photooxidation can be extended to flavin mononucleotide and flavin adenine dinucleotide. In addition, we report advanced synthesis; carboxymethylflavin was obtained by oxidation of formylmethylflavin with chlorite and hydrogen peroxide; lumichrome was obtained by heating of formylmethylflavin in 50% AcOH; lumiflavin was obtained by incubation of formylmethylflavin in 2 M NaOH, followed by isolation by step-by-step concentration.