1761-67-7Relevant articles and documents
Chang et al.
, p. 112 (1967)
Photolysis of Dimethylnitrosamine in the Gas Phase
Geiger, Georg,Huber, J. Robert
, p. 989 - 995 (1981)
Photodecomposition of dimethylnitrosamine in the gas phase ( 1 Torr) has been investigated following irradiation into the S1(n?*) 0(363.5 nm) and S2(??'*) 0(248.1 nm) transitions at room temperature.With a quantum yield of unity, excitation into the S1 state yields the fragments (CH3)2N and NO which then recombine leaving no photoproducts.The addition of O2 results in only one photoproduct, (CH3)2NNO2.Irradiating into the S2 state, the products CH2=N-CH3, (CH2=N-CH3)3, CH2=NOH, N2O, NO, H2, and N2 were identified by capillary gas chromatography mass spectrometry.In the presence of N2 as a buffer gas the photoproducts are only CH2=N-CH3, (CH2=N-CH3)3, N2O, and H2.For both excitation conditions a mechanism is proposed involving cleavage of the N,N-bond as the main primary photolytic process.
Stolkin et al.
, p. 327,328, 330, 331, 335 (1977)
Frost et al.
, (1978)
Meier et al.
, p. 1686 (1968)
Matrix-IR spectroscopic investigations of the thermolysis and photolysis of diazoamides
Wentrup, Curt,Bibas, Herve,Kuhn, Arvid,Mitschke, Ullrich,McMills, Mark C.
, p. 10705 - 10717 (2013/11/19)
Matrix photolysis of N,N-dialkyldiazoacetamides 1a-d at 7-10 K results in either the formation of C-H insertion products (in case of N,N-dimethyl and N,N-diethyl diazoamides) or almost exclusive Wolff rearrangement to ketenes (in the case of the cyclic di
A small molecule that mimics the metabolic activity of copper-containing amine oxidases (CuAOs) toward physiological mono- and polyamines
Largeron, Martine,Fleury, Maurice-Bernard,Strolin Benedetti, Margherita
supporting information; experimental part, p. 3796 - 3800 (2010/09/06)
Primary aliphatic biogenic amines have been successfully oxidized using a quinonoid species that mimics the metabolic activity of copper-containing amine oxidase (CuAO) enzymes. Especially, high catalytic performances were observed with aminoacetone, a threonine catabolite, and methylamine, a metabolite of adrenaline, and with the primary amino groups of putrescine and spermidine which are both decarboxylation products of ornithine and S-adenosyl-methionine. Furthermore, contrary to flavine adenine dinucleotide (FAD)-dependent amine oxidase enzymes, no activity was found toward secondary and tertiary amines.