Bagramyan K, Trchounian A
Department of Biophysics, Faculty of Biology, Yerevan State University, Yerevan, 375049, Armenia.
Biochemistry (Mosc). 2003 Nov;68(11):1159-70. doi: 10.1023/b:biry.0000009129.18714.a4.
Formate hydrogen lyase from Escherichia coli is a membrane-bound complex that oxidizes formic acid to carbon dioxide and molecular hydrogen. Under anaerobic growth conditions and fermentation of sugars (glucose), it exists in two forms. One form is constituted by formate dehydrogenase H and hydrogenase 3, and the other one is the same formate dehydrogenase and hydrogenase 4; the presence of small protein subunits, carriers of electrons, is also probable. Other proteins may also be involved in formation of the enzyme complex, which requires the presence of metal (nickel-cobalt). Its formation also depends on the external pH and the presence of formate. Activity of both forms requires F(0)F(1)-ATPase; this explains dependence of the complex functioning on proton-motive force. It is also possible that the formate hydrogen lyase complex will exhibit its own proton-translocating function.
来自大肠杆菌的甲酸氢裂解酶是一种膜结合复合物，可将甲酸氧化为二氧化碳和分子氢。在厌氧生长条件和糖类（葡萄糖）发酵过程中，它以两种形式存在。一种形式由甲酸脱氢酶H和氢化酶3组成，另一种形式是相同的甲酸脱氢酶和氢化酶4；也可能存在作为电子载体的小蛋白质亚基。其他蛋白质也可能参与酶复合物的形成，这需要金属（镍 - 钴）的存在。其形成还取决于外部pH值和甲酸的存在。两种形式的活性都需要F(0)F(1)-ATP酶；这解释了复合物功能对质子动力的依赖性。甲酸氢裂解酶复合物也有可能展现出自身的质子转运功能。
