Sebban C, Blanchard L, Bruschi M, Guerlesquin F
Unité de Bioénergétique et Ingénierie des Protéines, IFRC1, CNRS, Marseille, France.
FEMS Microbiol Lett. 1995 Nov 1;133(1-2):143-9. doi: 10.1111/j.1574-6968.1995.tb07875.x.
Formate dehydrogenase from Desulfovibrio vulgaris Hildenborough, a sulfate-reducing bacterium, has been isolated and characterized. The enzyme is composed of three subunits. A high molecular mass subunit (83,500 Da) is proposed to contain a molybdenum cofactor, a 27,000 Da subunit is found to be similar to the Fe-S subunit of the formate dehydrogenase from Escherichia coli and a low molecular mass subunit (14,000 Da) holds a c-type heme. The presence of heme c in formate dehydrogenase is reported for the first time and is correlated to the peculiar low oxidoreduction potential of the metabolism of these strictly anaerobic bacteria. In vitro measurements have shown that a monoheme cytochrome probably acts as a physiological partner of the enzyme in the periplasm.
已分离并鉴定了来自硫酸盐还原菌希登伯勒脱硫弧菌的甲酸脱氢酶。该酶由三个亚基组成。一个高分子量亚基（83,500道尔顿）被认为含有钼辅因子，一个27,000道尔顿的亚基被发现与大肠杆菌甲酸脱氢酶的铁硫亚基相似，而一个低分子量亚基（14,000道尔顿）含有一个c型血红素。首次报道了甲酸脱氢酶中存在血红素c，这与这些严格厌氧菌代谢特有的低氧化还原电位相关。体外测量表明，一种单血红素细胞色素可能在周质中作为该酶的生理伴侣发挥作用。
