Triazoles aminobenzotriazoles

The l-aminobenzotriazoles are desirable as benzyne precursors. The dianion of N-boc-1-aminobenzotriazole 34 reacts to introduce electrophiles at the 7 position to give 35 in excellent yields <96TL5615>. Pyrrolo[l,2-c][l,2,3]triazoles 37 are formed by trapping... 

The /V-nitration of 4-amino-1,2,4-triazole, 1-aminobenzimidazole, N-aminobenzotriazole [73JCS(P 1)2624] and l,3-diamino-l,2,3-triazolium salts (891ZV2654) have been reported. The nitramine products exist in the... 

Oxidation of heterocyclic amino derivatives yields various reaction products depending on the structure of the amine. 4-Benzylamino-3-methyl-4//-1,2,4-triazole is oxidized with DCT in chloroform to give the azomethine derivative 110 (69ZC325). l-Amino-4,5-diphenyl-l,2,3-triazole under the action of CBT forms diphenylacetylene 2-aminobenzotriazole yields cis, cw-l,4-dicyanobuta-l,3-diene and 1-aminobenzotriazole yields a mixture of chlorobenzene and o-dichlorobenzene. Oxidation of 1-aminobenzotriazole in the presence of tetraphenylcyclopentadienone leads to 1,2,3,4-tetraphenylnaphthalene via benzyne intermediate [68JCS(CC)1305 69JCS(C)1474] (Scheme 101). 

Aminobenzotriazole and related triazoles, all of which are aryne precursors, are autocatalytic inactivators of cytochrome P-450 and related oxidases. Evidence has been presented that the enzyme oxidizes these substrates to benzyne which then binds covalently to the heme prosthetic group of the enzyme, possibly as in 120, thus deactivating it. 

B enzyne and Cyclobutadlene Stereoelectronlc Activation - The catalytic interaction of cytochrome P-450 with 1-aminobenzotriazole (2), a compound that releases benzyne when chemically oxidized, results in time-dependent enzyme inactivation. 2,63 An unusual prosthetic heme adduct is formed in which two vicinal nitrogens of protoporphyrin IX are bridged by an ortho-substituted phenyl ring. The Inactivation reaction occurs even when substituents are placed on the exocyclic amino group of 1-amlnobenzo-triazole, although enzyme inactivation by substituted analogues has not been well characterized. The catalytic role of the enzyme and the structure of the heme adduct indicate that inactivation follows oxidative release of benzyne or a benzyne-like species within the active site of the enzyme. 

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