Chandrasekar R, Klapper M H
J Biol Chem. 1986 Mar 15;261(8):3616-9.
We describe a two-step purification of the methoxatin-containing enzyme methylamine dehydrogenase from crude extracts of the bacterium W3A1, and a longer purification of cytochrome c552 from the same organism. Some of the kinetic properties of the dehydrogenase are presented, together with the demonstration that c552 is an electron acceptor for this enzyme. Cytochrome c552 is the only hemeprotein we observed in the visible spectrum of intact W3A1 cells that were grown under the same culture conditions used for the protein purifications. Addition of methylamine to whole cells causes an increase in the rate of O2 uptake together with an abrupt reduction of c552. We propose that, in vivo, the electrons from the amine reach the hemeprotein through the dehydrogenase.
我们描述了从细菌W3A1的粗提物中两步纯化含甲氧喋呤的酶甲胺脱氢酶，以及从同一生物体中较长时间纯化细胞色素c552的过程。文中介绍了脱氢酶的一些动力学特性，并证明c552是该酶的电子受体。细胞色素c552是我们在与蛋白质纯化所用相同培养条件下生长的完整W3A1细胞的可见光谱中观察到的唯一血红素蛋白。向全细胞中添加甲胺会导致氧气摄取速率增加，同时c552突然还原。我们提出，在体内，来自胺的电子通过脱氢酶到达血红素蛋白。
