McConnell I L, Badger M R, Wydrzynski T, Hillier W
Research School of Biological Sciences, The Australian National University, Canberra, ACT 0200, Australia.
Biochim Biophys Acta. 2007 Jun;1767(6):639-47. doi: 10.1016/j.bbabio.2007.01.019. Epub 2007 Feb 7.
Using a carbonic anhydrase assay based on membrane inlet mass spectrometry (MIMS), we have extended our earlier investigations of Photosystem II (PSII)-associated carbonic anhydrase activity in spinach PSII preparations (W. Hillier, I. McConnell, M. R. Badger, A. Boussac, V.V. Klimov G. C. Dismukes, T. Wydrzynski Biochemistry 2006, 45:2094). The relationship between the carbonic anhydrase activity and O(2) evolution has been evaluated in terms of the effects of metal ion addition, preparation type, light, and response to specific inhibitors. The results indicate that the PSII-associated carbonic anhydrase activity is variable and appears not to be associated specifically with the oxygen evolving activity nor the 33 kDa extrinsic manganese stabilising protein.
利用基于膜进样质谱法(MIMS)的碳酸酐酶测定方法,我们扩展了之前对菠菜光系统II(PSII)制剂中与PSII相关的碳酸酐酶活性的研究(W.希利尔、I.麦康奈尔、M.R.巴杰、A.布萨克、V.V.克利莫夫、G.C.迪斯穆克斯、T.维德津斯基,《生物化学》,2006年,45卷:2094页)。已根据金属离子添加、制剂类型、光照以及对特定抑制剂的反应等影响因素,评估了碳酸酐酶活性与氧气释放之间的关系。结果表明,与PSII相关的碳酸酐酶活性是可变的,似乎与放氧活性或33 kDa外在锰稳定蛋白并无特定关联。