牛肝单胺氧化酶中黄素腺嘌呤二核苷酸的红细胞沉降率分析。

ESR analysis of the FAD in bovine liver monoamine oxidase.

作者信息

Tan A, Glantz M D, Piette L H, Yasunobu K T

出版信息

Biochem Biophys Res Commun. 1983 Dec 16;117(2):517-23. doi: 10.1016/0006-291x(83)91230-5.

Abstract

Two hydrazine spin labels, 1-oxyl-2,2,5,5-tetramethylpyrroline-3-carbonyl ethyl hydrazine and 1-oxyl-2,2,6,6-tetramethylpiperidino-4-hydrazine, were synthesized as probes of the FAD binding site of monoamine oxidase. The reporter nitroxide moiety showed an ESR spectrum classified as partially immobilized which is indicative of FAD near the surface of the enzyme. Attempts to pick up flavin semiquinone or free radical intermediates during substrate oxidation with the spin traps 5,5-dimethyl-1-pyrroline-1-oxidase and phenyl-t-butylnitrone were not successful.

摘要

合成了两种肼自旋标记物，即1-氧代-2,2,5,5-四甲基吡咯啉-3-羰基乙肼和1-氧代-2,2,6,6-四甲基哌啶基-4-肼，作为单胺氧化酶黄素腺嘌呤二核苷酸（FAD）结合位点的探针。报告氮氧自由基部分显示出归类为部分固定的电子自旋共振（ESR）谱，这表明FAD靠近酶的表面。在用自旋捕捉剂5,5-二甲基-1-吡咯啉-1-氧化物和苯基叔丁基硝酮进行底物氧化过程中，尝试捕捉黄素半醌或自由基中间体未成功。