黄嘌呤氧化酶与黄嘌呤和尿酸复合物的电子顺磁共振光谱学
Electron-paramagnetic-resonance spectroscopy of complexes of xanthine oxidase with xanthine and uric acid.
作者信息
Bray R C, Barber M J, Lowe D J
出版信息
Biochem J. 1978 Jun 1;171(3):653-8. doi: 10.1042/bj1710653.
Abstract
Molybdenum(V) e.p.r. signals from reduced functional milk xanthine oxidase molecules (the Rapid signals), obtained in the presence of purine substrates and products, were further investigated [cf. Bray & Vänngård, (1969) Biochem. J. 114, 725-734; Pick & Bray (1969) Biochem. J. 114, 735-742]. Xanthine forms two complexes with the enzyme that are believed to correspond to different orientations of the substrate molecule in the active site. Only one complex appears to undergo the catalytic reaction. Non-productive complexes, analogous to theone with xanthine, are not formed by 1-methylxanthine or purine. Uric acid forms more than one e.p.r.-detectable complex, one of which is analogous to the non-productive xanthine complex. The computer program used for handing the e.p.r. data is described briefly.
摘要
在嘌呤底物和产物存在的情况下获得的还原型功能性乳黄嘌呤氧化酶分子的钼（V）电子顺磁共振信号（快速信号）得到了进一步研究[参见布雷和万恩加德，（1969年）《生物化学杂志》114卷，725 - 734页；皮克和布雷（1969年）《生物化学杂志》114卷，735 - 742页]。黄嘌呤与该酶形成两种复合物，据信这两种复合物对应于底物分子在活性位点的不同取向。似乎只有一种复合物会发生催化反应。1 - 甲基黄嘌呤或嘌呤不会形成类似于与黄嘌呤形成的那种非生产性复合物。尿酸形成不止一种可通过电子顺磁共振检测到的复合物，其中一种类似于非生产性黄嘌呤复合物。简要描述了用于处理电子顺磁共振数据的计算机程序。
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Complex-formation between reduced xanthine oxidase and purine substrates demonstrated by electron paramagnetic resonance.电子顺磁共振证明还原型黄嘌呤氧化酶与嘌呤底物之间的复合物形成。
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