Nivière V, Forget N, Bovier-Lapierre G, Bonicel J, Hatchikian C
Laboratoire de Chimie Bactérienne (LCB), CNRS, BP 71, Marseille, France.
Biochimie. 1988 Feb;70(2):267-72. doi: 10.1016/0300-9084(88)90070-3.
The two subunits of the nickel-iron hydrogenase from Desulfovibrio gigas have been purified by preparative sodium dodecyl sulfate polyacrylamide gel electrophoresis and their amino acid compositions have been determined. The N-terminal sequences for 15 residues of the large subunit (Mr 62,000) and 25 residues of the small subunit (Mr 26,000), respectively, were established. The occurrence of several cysteine residues in the small subunit is discussed in relation with their possible role in the binding of the redox centers of the enzyme.
巨大脱硫弧菌的镍铁氢化酶的两个亚基已通过制备型十二烷基硫酸钠聚丙烯酰胺凝胶电泳进行了纯化，并测定了它们的氨基酸组成。分别确定了大亚基（Mr 62,000）15个残基和小亚基（Mr 26,000）25个残基的N端序列。讨论了小亚基中几个半胱氨酸残基的存在与其在酶的氧化还原中心结合中可能发挥的作用之间的关系。
