来自酵母毕赤酵母的黄素依赖性乙醇氧化酶。辅酶FAD在蛋白质结构中的空间定位：热氚轰击和电子自旋共振实验。
Flavin-dependent alcohol oxidase from the yeast Pichia pinus. Spatial localization of the coenzyme FAD in the protein structure: hot-tritium bombardment and ESR experiments.
作者信息
Averbakh A Z, Pekel N D, Seredenko V I, Kulikov A V, Gvozdev R I, Rudakova I P
机构信息
Institute of Chemical Physics, Russian Academy of Sciences, Moscow Region.
出版信息
Biochem J. 1995 Sep 1;310 ( Pt 2)(Pt 2):601-4. doi: 10.1042/bj3100601.
The spatial localization of the coenzyme FAD in the quaternary structure of the alcohol oxidase from the yeast Pichia pinus was studied by tritium planigraphy and ESR methods. In the present paper we measured the specific radioactivity of FAD labelled as a part of the alcohol oxidase complex. The specific-radioactivity ratio for two FAD portions (FMN and AMP) was calculated. ESR experiments show 4 A (0.4 nm) to be the depth of immersion of paramagnetic isoalloxazines into alcohol oxidase octamer molecules. It is suggested that FAD molecules are bound to the surface of the octamer, rather than to the subunit interfaces. The orientation of the prosthetic group FAD in the alcohol oxidase protein is discussed.
采用氚平面成像和电子自旋共振（ESR）方法研究了辅酶黄素腺嘌呤二核苷酸（FAD）在毕赤酵母酒精氧化酶四级结构中的空间定位。在本文中，我们测量了作为酒精氧化酶复合物一部分的标记FAD的比放射性。计算了两个FAD部分（黄素单核苷酸和腺苷一磷酸）的比放射性比率。ESR实验表明，顺磁性异咯嗪嵌入酒精氧化酶八聚体分子的深度为4埃（0.4纳米）。研究表明，FAD分子结合在八聚体表面，而非亚基界面。本文还讨论了辅基FAD在酒精氧化酶蛋白中的取向。
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