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卤化物与碳酸酐酶结合的X射线吸收研究。

X-ray absorption studies of halide binding to carbonic anhydrase.

作者信息

Brown G S, Navon G, Shulman R G

出版信息

Proc Natl Acad Sci U S A. 1977 May;74(5):1794-7. doi: 10.1073/pnas.74.5.1794.

Abstract

X-ray absorption measurements of bovine carbonic anhydrase B have been made at the the Stanford Synchrotron Radiation Project with a spectrometer operating in the fluorescence mode. Differences in absorption at and beyond the zinc K-edge near 9664 ev have been observed upon the addition of bromide or iodide. The additional absorption in k space, out to k approximately 7 A-1, obtained upon the addition of iodide has been compared with the absorption in this region of a ZnI2 sample. The similarities between these absorptions lead to the conclusion that the zinc-iodide distance in the protein is 2.65 +/-0.06 A; it is known to be 2.62 A in ZnI2. This shows that the iodide binds directly to the zinc in the protein.

摘要

利用在荧光模式下运行的光谱仪,在斯坦福同步辐射项目中对牛碳酸酐酶B进行了X射线吸收测量。在添加溴化物或碘化物后,观察到在9664电子伏特附近锌K边及以外区域的吸收差异。将添加碘化物后在k空间中直至k约为7 Å⁻¹处获得的额外吸收与ZnI₂样品在该区域的吸收进行了比较。这些吸收之间的相似性得出结论,蛋白质中锌-碘的距离为2.65±0.06 Å;已知在ZnI₂中该距离为2.62 Å。这表明碘化物直接与蛋白质中的锌结合。

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本文引用的文献

1
Inhibition by anions of human red cell carbonic anhydrase B: physiological and biochemical implications.
Science. 1976 Nov 12;194(4266):746-7. doi: 10.1126/science.194.4266.746.
3
Purification and properties of bovine erythrocyte carbonic anhydrase.牛红细胞碳酸酐酶的纯化及性质
Biochim Biophys Acta. 1960 Apr 8;39:218-26. doi: 10.1016/0006-3002(60)90156-6.
9
Carbonic anhydrase: chemistry, physiology, and inhibition.碳酸酐酶:化学、生理学及抑制作用
Physiol Rev. 1967 Oct;47(4):595-781. doi: 10.1152/physrev.1967.47.4.595.
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Interaction of cobalt(II)--carbonic anhydrase with anions.
Biochemistry. 1966 Aug;5(8):2641-6. doi: 10.1021/bi00872a023.

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