408328-24-5

Basic information

• Product Name: 1,2-Dimethyl-4-nitro-5-nitroso-benzene
• Synonyms: 1,2-Dimethyl-4-nitro-5-nitroso-benzene
• CAS NO: 408328-24-5
• Molecular Weight: 180.163
• Mol File: 408328-24-5.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: 1,2-Dimethyl-4-nitro-5-nitroso-benzene(CAS DataBase Reference)
• NIST Chemistry Reference: 1,2-Dimethyl-4-nitro-5-nitroso-benzene(408328-24-5)
• EPA Substance Registry System: 1,2-Dimethyl-4-nitro-5-nitroso-benzene(408328-24-5)

Safety Data

• Hazardous Substances Data: 408328-24-5(Hazardous Substances Data)

Upstream product

• 6972-71-0 4,5-dimethyl-2-nitrobenzenamine 

Downstream Products

• 195812-20-5 (S)-2-amino-N^α-(tert-butyloxycarbonyl)-6-(4',5'-dimethyl-2'-nitroanilin-N-yl)hexanoic acid 
• 195812-21-6 (S)-6-(2-Amino-4,5-dimethyl-phenylamino)-2-tert-butoxycarbonylamino-hexanoic acid 
• 610-23-1 4,5-dimethyl-1,2-dinitrobenzene 

Relevant articles and documents

Thiourea-enhanced flavin photooxidation of benzyl alcohol

Upon irradiation, flavin oxidises 4-methoxybenzyl alcohol to the corresponding aldehyde using aerial O2 as the terminal oxidant. We have observed that this reaction is significantly accelerated by the presence of thiourea. A series of thiourea-functionalised flavins has been prepared from flavin isothiocyanates and their photocatalytic efficiencies have been monitored by NMR. The alcohol photooxidation proceeds rapidly and cleanly with high turnover numbers of up to 580, exceeding previously reported performances. A likely mechanistic rationale for the more than 30-fold acceleration of the photo-redox reaction by thiourea has been derived from spectroscopic, electrochemical, and kinetic studies. Thus, thiourea acts as an electron-transfer mediator for the initial photooxidation of 4-methoxybenzyl alcohol by the excited flavins. This mechanism has similarities to electron-relay mechanisms in flavoenzymes, for which cysteine sulfenic acid intermediates are proposed. The observation that thiourea mediates flavin photo-redox processes is valuable for the design of more sophisticated photocatalysts based on Nature's best redox chromophore.

Towards artificial DNA-repair enzymes: Incorporation of a flavin amino acid into DNA-binding oligopeptides

Mimicking DNA photolyases: Model proteins containing the flavin amino acid L-1 within the DNA-binding domain of a transcription factor are capable of completely repairing damage from the formation of pyrimidine dimers in single-stranded oligonucleotides.