通过电子顺磁共振光谱法对醛氧化酶钼中心进行的研究。
Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum centre of aldehyde oxidase.
作者信息
Bray R C, George G N, Gutteridge S, Norlander L, Stell J G, Stubley C
出版信息
Biochem J. 1982 Apr 1;203(1):263-7. doi: 10.1042/bj2030263.
Molybdenum(V) e.p.r. spectra from reduced forms of aldehyde oxidase were obtained and compared with those from xanthine oxidase. Inhibited and Desulpho Inhibited signals from aldehyde oxidase were fully characterized, and parameters were obtained with the help of computer simulations. These differ slightly but significantly from the corresponding parameters for the xanthine oxidase signals. Rapid type 1 and type 2 and Slow signals were obtained from aldehyde oxidase, but were not fully characterized. From the general similarities of the signals from the two enzymes, it is concluded that the ligands of molybdenum must be identical and that the overall co-ordination geometries must be closely similar in the enzymes. The striking differences in substrate specificity must relate primarily to structural differences in a part of the active centre concerned with substrate binding and not involving the catalytically important molybdenum site.
获得了来自醛氧化酶还原形式的钼（V）电子顺磁共振光谱，并将其与黄嘌呤氧化酶的光谱进行了比较。对醛氧化酶的抑制和脱硫抑制信号进行了全面表征，并借助计算机模拟获得了参数。这些参数与黄嘌呤氧化酶信号的相应参数略有不同，但差异显著。从醛氧化酶获得了快速1型和2型以及慢速信号，但未对其进行全面表征。从两种酶信号的总体相似性可以得出结论，钼的配体必须相同，并且两种酶中的整体配位几何结构必须非常相似。底物特异性的显著差异主要与活性中心中与底物结合有关且不涉及催化重要钼位点的部分结构差异有关。
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