482-12-2

Upstream product

• 13345-95-4 1,5-dihydro-riboflavin 
• 1464-43-3 seleno-L-cystine 
• 83916-71-6 N-ribityl-3,4-dimethylaniline 
• 50-69-1 D-ribose 
• 95-64-7 4-amino-o-xylene 
• 67-52-7 BARBITURIC ACID 
• 21037-26-3 N-ribityl-2-phenylazo-4,5-dimethylaniline 

Downstream Products

• 146-17-8 O^5'-phosphono-riboflavin 
• 13345-95-4 1,5-dihydro-riboflavin 
• 1464-43-3 seleno-L-cystine 
• 752-56-7 5-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)pentane-1,2,3,4-tetrayl tetra butyrate 
• 21066-33-1 3-Methyl-tetra-O-acetyl-riboflavin 
• 1207984-66-4 tert-butyl 3,4-dichlorobenzyl(2-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)ethyl)carbamate 
• 1207984-31-3 4-((2-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)ethylamino)methyl)benzoic acid 
• 1207984-13-1 tert-butyl 2-(2-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)ethylamino)benzoate 
• 1207984-64-2 10-(2-(3,4-dichIorobenzylamino)ethyl)-7,8-dimethyIbenzo[g]pteridine-2,4(3H,10H)-dione 
• 1207984-12-0 2-(2-(7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl)ethylamino)benzoic acid 
• 6293-75-0 7,8-dimethyl-10-(2-thiosemicarbazono-ethyl)-isoalloxazine 
• 752-13-6 riboflavin 2',3',4',5'-tetra-acetate 

Relevant academic research and scientific papers

Studies on the reaction between reduced riboflavin and selenocystine

Selenocysteine (Sec) is a crucial component of mammalian thioredoxin reductase (TrxR) where it serves as a nucleophile for disulfide bond rupture in thioredoxin (Trx). Generation of the reduced state of Sec in TrxR requires consecutive two electron transfer steps, namely: (i) from NADPH to flavin adenine dinucleotide, (ii) from reduced flavin to the disulfide bond Cys59-S-S-Cys64, and finally (iii) from Cys59 and Cys64 to the selenosulfide bond Cys497-S-Se-Sec498. In this work, we studied the reaction between reduced riboflavin (RibH2) and selenocystine (Sec-Sec), an oxidized form of Sec. The interaction between RibH2 and Sec-Sec proceeded relatively slowly in comparison with its reverse reaction, that is, reduction of riboflavin (Rib) by Sec. The rate constant for the reaction between RibH2 and Sec-Sec was (7.9?±?0.1)?×?10?2?M?1 s?1 (pH 7.0, 25.0°C). The reaction between Rib and Sec proceeded via two steps, namely, a rapid reversible binding of Rib to Sec having a protonated selenol group to form a Sec-Rib complex, followed by nucleophilic attack of Sec-Rib by a second Sec molecule harboring a deprotonated selenol group. The equilibrium constant for the overall reduction process of Rib by Sec is (1.2?±?0.1)?×?106?M?1 (25.0°C). The finding that the interaction of RibH2 with oxidized selenol is reversible with its equilibrium favored toward the reverse reaction provides an additional explanation for the exceptional mechanism of the mammalian Trx/TrxR system involving transient reduction of a disulfide bond.

Site-Selective Synthesis of 15N- and 13C-Enriched Flavin Mononucleotide Coenzyme Isotopologues

Flavin mononucleotide (FMN) is a coenzyme for numerous proteins involved in key cellular and physiological processes. Isotopically labeled flavin is a powerful tool for studying the structure and mechanism of flavoenzyme-catalyzed reactions by a variety of techniques, including NMR, IR, Raman, and mass spectrometry. In this report, we describe the preparation of labeled FMN isotopologues enriched with 15N and 13C isotopes at various sites in the pyrazine and pyrimidine rings of the isoalloxazine core of the cofactor from readily available precursors by a five-step chemo-enzymatic synthesis.