Pearson D M, O'Reilly C, Colby J, Black G W
School of Health Sciences, University of Sunderlund, UK.
Biochim Biophys Acta. 1994 Dec 30;1188(3):432-8. doi: 10.1016/0005-2728(94)90066-3.
Pseudomonas thermocarboxydovorans strain C2 is capable of using carbon monoxide as the sole source of carbon and energy. The key enzyme for CO utilisation is the molybdenum containing iron-flavoprotein carbon monoxide dehydrogenase (CODH). This paper reports the DNA sequencing of a 4.7 kb region of the C2 genome which appears to encode the CODH enzyme. The genes for the three subunits of CODH, which we have named cut A, B and C, have been identified and they appear to form an operon. The predicted protein sequences of the three subunits have homology to the structurally related protein, xanthine dehydrogenase, from Drosophila melanogaster. By comparison with xanthine dehydrogenase it can be predicted that the molybdenum cofactor binds to the large subunit of CODH, the small subunit of CODH contains the iron-sulphur centers and the medium subunit binds FAD/NAD+.
嗜热羧基营养假单胞菌C2菌株能够将一氧化碳作为唯一的碳源和能源。利用一氧化碳的关键酶是含钼的铁黄素蛋白一氧化碳脱氢酶（CODH）。本文报道了C2基因组中一个4.7 kb区域的DNA测序结果，该区域似乎编码CODH酶。已鉴定出CODH三个亚基的基因，我们将其命名为cut A、B和C，它们似乎形成一个操纵子。这三个亚基的预测蛋白质序列与黑腹果蝇中结构相关的蛋白质黄嘌呤脱氢酶具有同源性。通过与黄嘌呤脱氢酶比较，可以预测钼辅因子与CODH的大亚基结合，CODH的小亚基含有铁硫中心，中等亚基结合FAD/NAD+。
